| utilization of nitrogen compounds and ammonia assimilation by chromatiaceae. | chromatium vinosum strain d, thiocapsa roseopersicina strain 6311 and ectothiorhodospira mobilis strain 8112 were grown anaerobically in the light with various single nitrogen sources. when substituted for nh4cl only glutamine and casamino acids supported good growth of all strains tested. peptone and urea were utilized by c. vinosum and t. roseopersicina, glutamate, asparagine and nitrate only by c. vinosum. the strains were able to grow with molecular nitrogen; complete inhibition of this grow ... | 1977 | 19002 |
| [use of urea by purple bacteria]. | strains of purple sulfur bacteria (chromatium minutissimum, ectothiorhodospira shaposhnikovii, thiocapsa roseopersicina, lamprobacter modestohalophilus) and nonsulfur bacteria (rhodopseudomonas palustris, rh. spheroides, rhodospirillum rubrum) grow in media containing urea as a source of nitrogen at concentrations from 0.5 to 5.0%. they can also utilize the carbon of urea and thus grow in the absence of bicarbonate. urea is decomposed by all the studied purple bacteria with the participation of ... | 1979 | 112359 |
| short-lived delayed luminescence of photosynthetic organisms. i. nanosecond afterglows in purple bacteria at low redox potentials. | a combined study of emissions of purple bacteria rhodospirillum rubrum, ectothiorhodospira shaposhnikovii and thiocapsa roseopersicina was performed under conditions of low potential. it has been shown that a considerable part of the emission represents a delayed luminescence with a lifetime of about 5 ns and an activation energy delta e = 0.05 +/- 0.03 ev. intensity of this delayed luminescence is approximately equal to that of prompt fluorescence. it diminishes as temperature decreases and als ... | 1979 | 116682 |
| ferredoxin-linked nitrate reductase from the phototrophic bacterium ectothiorhodospira shaposhnikovii. | | 1975 | 166876 |
| [possible pathways for acetyl-coa formation by purple bacteria]. | purple sulfur (ectothiorhodospira shaposhnikovii, chromatium minutissimum, lamprobacter modestohalophilus, thiocapsa roseopersicina) and nonsulfur (rhodospirillum rubrum, rhodopseudomonas palustris, rhodopseudomonas spheroides) bacteria are capable of forming acetyl-coa synthetase, phosphotransacetylase and acetokinase independent of the medium composition and growth conditions. in all of the purple sulfur bacteria with an exception of e. shaposhnikovii, the activity of acetokinase is much highe ... | 1979 | 228168 |
| [carbonic anhydrase activity of phototropic bacteria]. | the activity of carboanhydrase was assayed in seven species of phototrophous bacteria: three species of the rhodospirillaceae genus, three species of the chromatiaceae genus, and one species of the chlorobiaceae genus. the activity of carboanhydrase was found in five species among seven. it decreased on passing from photoautotrophous to photoheterotrophous conditions of growth, and then to dark heterotrophous conditions, which correlated with the activity of the calvin cycle in the bacteria. no ... | 1977 | 408582 |
| [growth of ectothiorhodospira shaposhnikovii on media with various sulfur compounds]. | ectothiorhodospira shaposhnikovii, strain 1, can use thiosulphate, sulphide, sulphite, sulphate, cystein, methionine and glutathione as a source of sulphur during its growth in the light and in the dark. thiosulphate, sulphide and sulphite are used by the bacterium also as electron donors in photosynthesis so that it can grow in anaerobic autotrophic conditions. growth of the cultures in the presence of various sulphur compounds depends on the concentration of sodium and potassium salts in the m ... | 1979 | 440157 |
| new experimental approach to the estimation of rate of electron transfer from the primary to secondary acceptors in the photosynthetic electron transport chain of purple bacteria. | a method for calculating the rate constant (ka1a2) for the oxidation of the primary electron acceptor (a1) by the secondary one (a2) in the photosynthetic electron transport chain of purple bacteria is proposed. the method is based on the analysis of the dark recovery kinetics of reaction centre bacteriochlorophyll (p) following its oxidation by a short single laser pulse at a high oxidation-reduction potential of the medium. it is shown that in ectothiorhodospira shaposhnikovii there is little ... | 1976 | 816385 |
| [carbohydrate metabolism enzymes of purple sulfur-bacteria during growth in the dark]. | ectothiorhodospira shaposhnikovii, chromatium minutissimum and thiocapsa roseopersicina were grown in the dark under anaerobic conditions on media containing glucose or fructose and organic acids. their cell contained the following enzymes of the fructose diphosphate pathway: phosphofructokinase, fructose diphosphate aldolase, and 3-phosphoglyceraldehyde dehydrogenase. the activity of fructose diphosphate aldolase was higher in the cells grown in the dark than in the cells grown in the light. th ... | 1977 | 882007 |
| [growth conditions for ectothiorhodospira shaposhnikovii in the presence of oxygen in the dark]. | | 1976 | 940493 |
| molecular and catalytic properties of ribulose 1,5-bisphosphate carboxylase from the photosynthetic extreme halophile ectothiorhodospira halophila. | d-ribulose 1,5-bisphosphate (rubp) carboxylase has been purified from the photosynthetic extreme halophile ectothiorhodospira halophila. despite a growth requirement for almost saturating sodium chloride in the medium, both crude and homogeneous preparations of rubp carboxylase obtained from this organism were inhibited by salts. sedimentation equilibrium analyses showed the enzyme to be large (molecular weight: 601,000). the protein was composed of two types of polypeptide chains of 56,000 and ... | 1976 | 947890 |
| energy coupling in the active transport of proline and glutamate by the photosynthetic halophile ectothiorhodospira halophila. | when illuminated, washed cell suspensions of ectothiorhodospira halophila carry out a concentrative uptake of glutamate or proline. dark-exposed cells accumulate glutamate but not proline. proline transport was strongly inhibited by carbonylcyanide-m-chlorophenylhydrazone (cccp), a proton permeant that uncouples photophosphorylation, and by 2-heptyl-4-hydroxyquinoline-n-oxide (hqno), an inhibitor of photosynthetic electron transport. a stimulation of proline uptake was effected by n,n'-dicyclohe ... | 1976 | 956126 |
| [growth of purple sulfur bacteria in the dark in anaerobic conditions]. | phototrophic sulphur bacteria chromatium minutissimum 1 c, ectothiorhodospira shaposhnikovii 1, and various strains of thiocapsa roseopersicina grow in the dark under anaerobic conditions (hydrogen or argon) on organic media in the presence of sulphide, thiosulphate or molecular sulphur. ect. shaposhnikovii grows also in the presence of sulphite, cysteine, methionine, glutathione, and, to a less degree, sulphates. cultures of ect. shaposhnikovii growing in the dark under anaerobic conditions ass ... | 1976 | 979675 |
| [fractionation of sulfur isotopes by phototrophic sulfur bacterium ectothiorhodospira shaposhnikovii]. | two processes of sulphur isotope fractionation have been found in experiments with the sulphur purple bacterium ectothiorhodospira shaposhnikovii. as a result, a light isotope, 32s, is concentrated in residual hydrogen sulphide, and a heavy isotope, 34s, in elementary suphur which is deposited outside the cell. the sulphate produced is lighter than elementary sulphur. fractionation of sulphur isotopes is observed in natural conditions and is confined to places of mass growth of photosynthetic su ... | 1976 | 1004261 |
| [acetate photometabolism in ectothiorhodospira shaposhnikovii]. | the cells of ectothiorhodospira were cultivated under autotrophic conditions and assimilated 14c-acetate in the presence of bicarbonate. the label was incorporated rapidly into phosphoglyceric acid (pga) and phosphorous esters (pe) of sugars, into compounds of the tricarboxylic acid cycle (tac), aspartate, glutamate. after some time the content of the label became the highest in glutamate and decreased in other compounds. the same products were formed upon the assimilation of acetate by the cell ... | 1975 | 1226131 |
| structure and composition of intracytoplasmic membranes of ectothiorhodospira mobilis. | the lamellar membrane stacks of ectothiorhodospira mobilis were isolated and purified by a combination of lysozyme and osmotic shock treatment, followed by differential and density gradient centrifugation. preparations of lamellar membranes were enriched at least 2.4-fold in the ratio of bacteriochlorophyll a to protein. thin-sectioning, negative staining, platinum-carbon shadowing and freeze-etching were used to study the architecture of the membrane units. both platinum-carbon shadowing and fr ... | 1976 | 1259516 |
| three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium rhodocyclus tenuis determined and refined at 1.5 a resolution. | the molecular structure of the high-potential iron-sulfur protein (hipip) isolated from the phototrophic bacterium, rhodocyclus tenuis, has been solved and refined to a nominal resolution of 1.5 a with a crystallographic r-factor of 17.3% for all measured x-ray data from 30 a to 1.5 a. it is the smallest of the hipip structures studied thus far with 62 amino acid residues. crystals used in the investigation belonged to the space group p2(1) with unit cell dimensions of a = 36.7 a, b = 52.6 a, c ... | 1992 | 1453470 |
| the primary structure of the antenna polypeptides of ectothiorhodospira halochloris and ectothiorhodospira halophila. four core-type antenna polypeptides in e. halochloris and e. halophila. | antenna polypeptides from two species of the family ectothiorhodospiraceae have been investigated. by means of gel filtration and subsequent high-performance liquid chromatography, at least five polypeptides were isolated from each of ectothiorhodospira halochloris and ectothiorhodospira halophila. the majority of their primary structures was identified by edman degradation. comparison of these polypeptide sequences with the known primary structures of antenna polypeptides from various purple no ... | 1992 | 1577009 |
| 1h-nmr studies of high-potential iron-sulfur protein from the purple phototrophic bacterium, rhodospirillum tenue. | the high-potential iron-sulfur protein (hipip) from rhodospirillum tenue (strain 3761) shows only a weak (20-25%) sequence similarity to hipips from chromatium vinosum, ectothiorhodospira halophila and ectothiorhodospira vacuolata, including the strict conservation of only two of the twelve residues assumed to be in the 4fe-4s cluster packing region [tedro, s. m., meyer, t. e. and kamen, m. d. (1979) j. biol. chem. 254, 1495-1500]. in spite of these differences, the general range and distributio ... | 1989 | 2714284 |
| hydrogenases of phototrophic microorganisms. | this review surveys recent work done in the laboratory of the author and related laboratories on the properties and possible practical applications of hydrogenases of phototrophic microorganisms. homogeneous hydrogenase preparations were obtained from purple non-sulfur (rhodospirillum rubrum s1, rhodobacter capsulatus b10) and purple sulfur (chromatium vinosum d, thiocapsa roseopersicina bbs) bacteria, and from the green sulfur bacterium chlorobium limicola forma thiosulfatophilum l; highly puri ... | 1986 | 3015244 |
| laser flash photolysis studies of electron transfer between ferredoxin-nadp+ reductase and several high-potential redox proteins. | complex formation and the kinetics of electron transfer between ferredoxin-nadp+ reductase (fnr) and two structurally homologous acidic 4fe-4s high-potential ferredoxins (hipip's) from ectothiorhodospira halophila (hp1 and hp2) and two structurally homologous cytochromes c2 from paracoccus denitrificans and rhodospirillum rubrum (pc2, and rc2, respectively) have been investigated by gel filtration and laser flash photolysis techniques. gel filtration studies indicated that complex formation occu ... | 1987 | 3032236 |
| ctothiorhodospira halophila: a new species ofthe genus ectothiorhodospira. | | 1969 | 4192367 |
| [effect of acetate on oxidation of hydrogen sulfide and photoassimilation of carbon dioxide by ectothiorhodospira shaposhnikovii]. | | 1972 | 4657968 |
| light intensity as regulator of photoinduced conversions in cytochromes during photosynthesis in ectothiorhodospira shaposhnikovii. | | 1972 | 4670413 |
| regulatory action of near uv light on the development of ectothiorhodospira shaposhnikovii carotenoids as possible sensitizing pigments. | | 1974 | 4838489 |
| [metabolism of propionate in ectothiorhodospira shaposhnikovii]. | | 1974 | 4849168 |
| [growth of the photosynthetizing bacteria ectothiorhodospira shaposhnikovii in the dark in aerobic conditions]. | | 1972 | 5044887 |
| on the interaction of photoactive bacteriochlorophyll with the primary electron acceptor in the reaction centre of ectothiorhodospira shaposhnikovii. | | 1972 | 5049016 |
| [effect of light spectral composition on growth, protein biosynthesis and some primary photosynthetic reactions in ectothiorhodospira shaposhnikovii]. | | 1972 | 5059131 |
| carotenoid composition in the genus ectothiorhodospira pelsh. | | 1971 | 5126867 |
| [effect of nitrogen source in the culture medium on the capability for nitrogen fixation and the mossbauer spectra of ectothiorhodospira shaposhnikovii cells]. | | 1971 | 5128687 |
| [effect of electron donors on the oxidation-reduction state of the electron-transport chain of ectothiorhodospira shaposhnikovii]. | | 1971 | 5130745 |
| [the kinetics of photo-induced transformation of cytochromes by ectothiorhodospira shaposhnikovu]. | | 1970 | 5493670 |
| ectothiorhodospira mobilis pelsh, a photosynthetic sulfur bacterium depositing sulfur outside the cells. | from salt flats on the galapagos islands, two strains of a red photosynthetic bacterium were isolated and identified as ectothiorhodospira mobilis, an organism first described by pelsh in 1937. the cells are curved in a short spiral, 0.7 to 1.0 mu wide and 2.0 to 4.8 mu long. they are motile by a polar tuft of flagella. cells contain several large stacks of lamellar membranes, carrying the pigments bacteriochlorophyll a and carotenoids of the spirillo xanthin series. cell division occurs by bina ... | 1968 | 5650091 |
| fine structure of ectothiorhodospira mobilis pelsh. | the cell wall structure, arrangement of photosynthetic membranes, and the attachment of flagella of ectothiorhodospira mobilis strain 8112 were examined by using freeze-etching and conventional electron microscopic techniques. the outer coat of the multilayered cell wall is comprised of 50 a repeating subunits, arranged in a regular array. the photosynthetic membranes, which originate from and are attached to the plasma membrane, are arranged in a more complex pattern than previously seen in oth ... | 1968 | 5669908 |
| [enzymes of carbohydrate metabolism in phototrophic bacteria]. | purple sulphur bacteria (chromatium minutissimum, ectothiorhodospira shaposhnikovii, thiocapsa roseopersicina), non-sulphur bacteria (rhodopseudomonas palustris rh. viridis), and green sulphur bacteria (chlorobium limicola f. thiosulfatophillum) contain all enzymes of the fructose diphosphate pathway of carbohydrate transformation, and also glucose-6-phosphate dehydrogenase. the activity of fructose diphosphate aldolase, triose phosphate dehydrogenase, and glucose-6-phosphate dehydrogenase incre ... | 1975 | 125844 |
| fine structure of ectothiorhodospira mobilis strain 8113 thylakoids: chemical fixation and freeze-etching studies. | | 1968 | 5711185 |
| oxido-reduction of b800-850 and b880 holochromes isolated from three species of photosynthetic bacteria as studied by electron-paramagnetic resonance and optical spectroscopy. | certain redox properties of bacteriochlorophyll alpha were used to probe the structure of several light-harvesting pigment-protein complexes or holochromes. to attribute redox properties unequivocally to a given holochrome, we worked with purified holochromes. we developed purification procedures for the b880 holochromes from rhodospirillum rubrum, rhodopseudomonas sphaeroides and ectothiorhodospira sp. and for the b800-850 holochromes from the latter two species. in all these holochromes, bacte ... | 1984 | 6086349 |
| short-lived delayed luminescence of photosynthesizing organisms. ii. the ratio between delayed and prompt fluorescence as studied by the modulation method. | the ratio between the intensities of delayed and prompt fluorescence was studied for different photosynthetic objects under different conditions by modulation method. the method is based on excitation of luminescing objects by light, modulated harmonically, and on a combined study of phase shifts and demodulation coefficients of the luminescence as related to excitation light. the presence of intense delayed emissions was revealed in purple bacteria, ectothiorhodospira shaposhinokovii, rhodospir ... | 1980 | 6768385 |
| [growth of ectothiorhodospira mobilis in the dark]. | the purple photosynthetic bacterium ectothiorhodospira mobilis, like e. shaposhnikovii, can grow in the dark in the presence of oxygen on organic media, in particular, containing acetate or malate. the source of sulfur may be sulfate or thiosulfate. the two bacteria grown in the light and in the dark display the activity of all the enzymes of the citric acid cycle, with the exception of alpha-ketoglutarate dehydrogenase, and possess the enzymes of the glyoxylate shunt (isocitrate lyase and malat ... | 1980 | 6771498 |
| [propionate metabolism of ectothiorhodospira shaposhnikovii during growth in the dark]. | assimilation of propionate by ectothiorhodospira shaposhnikovii growing under the aerobic conditions in the dark, like in the light involves carboxylation of propionyl-coa with the participation of biotin-dependent carboxylase. the succinate being formed is transformed in the reactions of the citric acid cycle and the glyoxylate shunt. this is corroborated by the determination of the enzyme activity manifested by cell extracts, by the composition and kinetics of labeled products, as well as by t ... | 1980 | 6777640 |
| [carbamyl phosphate and citrulline formation by phototrophic bacteria]. | the purple bacteria ectothiorhodospira shaposhnikovii and rhodospirillum rubrum are capable of synthesizing citrulline in the presence of ammonium hydrocarbonate, ornithine, atp and mg2+ ions. citrulline biosynthesis by these phototrophic bacteria is presumed to be catalysed by carbamate kinase and ornithine transcarbamoylase. therefore, certain phototrophic bacteria can assimilate carbon dioxide and ammonia for biosynthesis of amino acids, in particular, citrulline and, apparently, arginine. | 1981 | 6798373 |
| [kinetics of light-induced redox changes of high-potential cytochrome in the chromatophores of purple sulfur bacteria ectothiorhodospira shaposhnikovii]. | light-induced redox changes of high-potential cytochrome ch (em 7.0 = + 290 mv) have been studied. it was found that after switching off the actinic light there is a delay in the cytochrome dark reduction. the extent of the delay depends on the intensity of actinic light, being the more the higher the intensity. a simple kinetic model is proposed to explain both kinetics of redox changes of the cytochrome and dependence of the delay upon the intensity of actinic light. | 1982 | 6297620 |
| [thermodynamic characteristics of the interaction of high-potential cytochrome with dimer of bacteriochlorophyll in the reaction centers of ectothiorhodospira shaposhnikovii chromatophores]. | kinetics of dark reduction of cytochrome ch (e7=290 mv) after its photoinduced oxidation chromatophores of e. shaposhnikovii at 110-210 k is analysed. a ratio is derived which describes dark reduction of cytochrome. this ratio makes it possible to determine the value of free energy of the electron transfer between cytochrome and bacteriochlorophyll dimer of the reaction centre (bchl)2. the values of enthalpy and entropy of the transition under study at the temperatures below 210 k are equal to 1 ... | 1982 | 6291630 |
| [role of sodium ions in the absorption of c4-dicarboxylic acids by ectothiorhodospira shaposhnikovii]. | the uptake of c4-dicarboxylic acids by the phototrophic purple bacterium ectothiorhodospira shaposhnikovii, strain 1k, involves a common transport system obligatorily dependent on sodium ions. the values of km for the transport of succinate, malate and fumarate are 1-10(-7), 3-10(-7) and 8-10(-7) m, respectively. the transport of c4-dicarboxylic acids in an energy-dependent process; it is inhibited by m-chlorocarbonylcyanide phenylhydrazone. it has been proved that the uptake of c4-dicarboxylic ... | 1980 | 7393003 |
| [acetate metabolism in ectothiorhodospira shaposhnikovii growing in the dark]. | when the cells of ectothiorhodospira shaposhnikovii assimilated 1- and 2-14c-acetate for a short period of time in the dark under aerobic conditions, the greatest amount of 14c was found after 5 sec in malate, succinate and aspartate. the content of 14c in these compounds decreased in due time, but increased in phosphoglyceric acid and in phosphoric esters of sugars, citrate, alanine and glutamate. the composition and kinetics of labeled products formed during the assimilation of 14c-acetate by ... | 1980 | 7402118 |
| [ectothiorhodospira shaposhnikovii respiration when growing in light and in darkness]. | the respiration of the purple phototrophic bacterium ectothiorhodospira shaposhnikovii grown in the light under the anaerobic conditions or in the dark in the presence of oxygen is stimulated with sulfide, nnnn-tetramethyl-p-phenylenediamine (tmpd) + ascorbate and, to a less extent, organic substrates. the electron transport system of the organism is characterized by weak activities of nadh- and nadph-oxidoreductases and a weak activity of the oxidase region. the respiration of intact cells in t ... | 1980 | 7412613 |
| the oxidation rate of high-potential c-type cytochrome in the photochemical reaction centre is temperature-independent. | the temperature dependence of laser-induced (694.3 nm, 30 ns, 10 mj.cm-2) high-potential cytochrome c (em=+290 mv) oxidation kinetics was studied in ectothiorhodospira shaposhnikovii chromatophores. it was shown that the rate constant of this reaction is independent of temperature in the range of 300 k to 120 k. | 1980 | 6243964 |
| [formation and consumption of stored products by ectothiorhodospira shaposhnikovii]. | | 1971 | 5580117 |
| influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: evidence for the existence of two groups. | we have investigated the hipips from ectothiorhodospira vacuolata (iso-1 and iso-2), chromatium vinosum, rhodocyclus gelatinosus, rhodocyclus tenuis (strain 2761), rhodopila globiformis, and rhodospirillum salinarum (iso-2) by direct electrochemistry. using a glassy carbon electrode with a negatively charged surface, direct, unpromoted electrochemistry is possible with the positively charged hipips. with the negatively charged hipips, the positively charged and flexible bridging promoter poly(l- ... | 1995 | 7578075 |
| study of ectothiorhodospira shaposhnikovii. intracellular cytochrome oxidation reactions induced by ruby laser flashes. | | 1971 | 5154980 |
| [carbon dioxide assimilation pathways of ectothiorhodospira shaposhnikovii]. | | 1974 | 4828739 |
| [regulatory and substrate role of light in the development of ectothiorhodospira shaposhnikovii]. | | 1973 | 4790717 |
| amino acid sequence of high-redox-potential ferredoxin (hipip) isozymes from the extremely halophilic purple phototrophic bacterium, ectothiorhodospira halophila. | the amino acid sequences of high-redox-potential ferredoxin (hipip) isozymes from ectothiorhodospira halophila have been determined. these are: isozyme i, epraedghahdyvneaadpshgryqegqlcencafwgeavqdgwgrcthpdfdevlvkaegwcsvyapa s, and isozyme ii, glpdgvedlpkaeddhahdyvndaadtdharfqegqlcencqfwvdyvngwgycqhpdftdvlvrgegw csvyapa. isozyme ii is the major form of hipip produced by the bacterium (65-80%) and is the most acidic of the known hipips. the two isozymes are 72% identical to one another and requir ... | 1985 | 4037807 |
| hydrogen-1 nuclear magnetic resonance investigation of high-potential iron-sulfur proteins from ectothiorhodospira halophila and ectothiorhodospira vacuolata: a comparative study of hyperfine-shifted resonances. | proton nmr spectra of the oxidized and reduced forms of high-potential iron-sulfur proteins (hipips) were recorded at 200 mhz. the proteins studied were the hipips i and ii from ectothiorhodospira halophila and ectothiorhodospira vacuolata. hyperfine-shifted peaks in spectra of the oxidized proteins were assigned to some of the protons of the cysteinyl ligands and aromatic residues at the active site on the basis of their chemical shifts, longitudinal relaxation times, and temperature-dependent ... | 1986 | 3954994 |
| circular dichroism and redox properties of high redox potential ferredoxins. | the circular dichroism (cd) spectra of 13 examples of high-potential iron-sulfur proteins (hipips), a class of [4fe-4s] ferredoxins, have been determined. in contrast to the proposal of carter [carter, c. w., jr. (1977) j. biol. chem. 252, 7802-7811], no strict correlation between visible cd features and utilization of the [4fe-4s]2+/[4fe-4s]3+ oxidation levels was found. although most hipips have these features, the model requires their presence in all species. there is also no simple relations ... | 1985 | 3925987 |
| 1h and 13c nmr assignments and structural aspects of a ferrocytochrome c-551 from the purple phototrophic bacterium ectothiorhodospira halophila. | two-dimensional nuclear magnetic resonance was used to assign the 1h and 13c resonances of ferrocytochrome c-551 from ectothiorhodospira halophila, a halophilic phototrophic purple bacterium. this 78-residue protein belongs to a small subgroup of class i cytochromes c together with the analogous cytochromes c-551 from e. halochloris and e. abdelmalekii. a nearly complete assignment of 13c resonances was obtained at natural abundance using a gradient-enhanced 1h-detected heteronuclear single quan ... | 1995 | 7851392 |
| 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid. a novel cyclic amino acid from halophilic phototrophic bacteria of the genus ectothiorhodospira. | a novel cyclic amino acid was detected in and subsequently isolated from extremely halophilic species of the bacterial genus ectothiorhodospira. the structure of this new compound was elucidated by a combination of nuclear magnetic resonance (nmr) techniques and mass spectrometry. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid is only accumulated within the cytoplasm under certain growth conditions and seems to serve an osmoregulatory function. there is no previous reference to this mol ... | 1985 | 3838936 |
| properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. | a water-soluble yellow protein, previously discovered in the purple photosynthetic bacterium ectothiorhodospira halophila, contains a chromophore which has an absorbance maximum at 446 nm. the protein is now shown to be photoactive. a pulse of 445-nm laser light caused the 446-nm peak to be partially bleached and red-shifted in a time less than 1 microsecond. the intermediate thus formed was subsequently further bleached in the dark in a biphasic process occurring in approximately 20 ms. finally ... | 1987 | 3828315 |
| the nucleotide sequences of the 5s rrnas from the purple bacteria ectothiorhodospira halophila and ectothiorhodospira vacuolata. | | 1987 | 3822810 |
| crystallization of a high potential iron-sulfur protein from the halophilic phototrophic bacterium ectothiorhodospira halophila. | crystals of the high-potential iron-sulfur protein from ectothiorhodospira halophila strain bn 9626 have been grown from 3.4 to 3.5 m ammonium sulfate solutions at ph 7.5. the crystals belong to the space group p21 with unit cell dimensions of a = 60.00 a, b = 31.94 a, c = 40.27 a, and beta = 100.5 degrees. there are 2 molecules/asymmetric unit. the crystals diffract to at least 1.8 a, are stable in the x-ray beam, and are suitable for a high resolution x-ray crystallographic analysis. | 1986 | 3771550 |
| crystallographic characterization of a photoactive yellow protein with photochemistry similar to sensory rhodopsin. | a photoactive yellow protein purified from the phototrophic bacterium ectothiorhodospira halophila, has been crystallized by vapor diffusion from ammonium sulfate solution. the hexagonal crystals are in space group p6(3) with unit cell dimensions a = b = 66.89, c = 40.68 a and appear to have one 15,000-dalton protein in the asymmetric unit. photoactive yellow protein contains a chromophore with retinal-like properties; its color can be reversibly bleached, by visible light, with kinetics similar ... | 1986 | 3759993 |
| [kinetic model of the effect of dehydration on electron transfer from membrane-bound cytochrome c to the photosynthetic reaction center]. | amplitude characteristics and kinetics of laser-induced oxidation of high-potential cytochrome ch by a photosynthetic reaction center (rc) were investigated in ectothiorhodospira shaposhnikovii chromatophore preparations of various humidity. it is shown that the diminuition of the amount of oxidized cytochrome and the decrease of the rate of the reaction on lowering the preparation humidity can be explained in terms of the concept of conformation-controlled electron transfer within the ch-rc com ... | 1985 | 2993853 |
| anaerobic bacteria from hypersaline environments. | strictly anaerobic halophiles, namely fermentative, sulfate-reducing, homoacetogenic, phototrophic, and methanogenic bacteria are involved in the oxidation of organic carbon in hypersaline environments. to date, six anaerobic fermentative genera, containing nine species, have been described. two of them are homoacetogens. six species belong to the family haloanaerobiaceae, as indicated by their unique 16s rrna oligonucleotide sequences. desulfohalobium retbaense and desulfovibrio halophilus repr ... | 1994 | 8177169 |
| isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium ectothiorhodospira halophila. | a cytochrome c-551 and a pair of 'high redox-potential' ferredoxins (iso-high-potential iron-sulfur proteins) were found to be the major soluble electron-transport proteins in ectothiorhodospira halophila. smaller amounts of 'bacterial' ferredoxin and cytochrome c' were also observed. with the exception of cytochrome c-551, these proteins are commonly encountered in the purple sulfur bacteria, family chromatiaceae and less frequently in the purple bacteria, family rhodospirillaceae. in addition ... | 1985 | 2981543 |
| photoactive yellow protein from the purple phototrophic bacterium, ectothiorhodospira halophila. quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery. | a water-soluble yellow protein from e. halophila was previously shown to be photoactive (meyer, t. e., e. yakali, m. a. cusanovich, and g. tollin. 1987. biochemistry. 26:418-423). pulsed laser excitation in the protein visible absorption band (maximum at 445 nm) causes a rapid bleach of color (k = 7.5 x 10(3) s-1) followed by a slower dark recovery (k = 2.6 s-1). this is analogous to the photocycle of sensory rhodopsin ii from halobacterium (which also has k = 2.6 s-1 for recovery). we have now ... | 1989 | 2790139 |
| electron self-exchange in high-potential iron-sulfur proteins. characterization of protein i from ectothiorhodospira vacuolata. | during previous research on oxidized and reduced high-potential iron-sulfur proteins (hipip hereafter), qualitative different electron self-exchange rates were noticed. we have now investigated this phenomenon in detail for hipip i and ii from ectothiorhodospira vacuolata, which differ significantly in total charge and in which the sequence homology is the largest among all known hipips. we have also characterized the electronic structure of hipip i through 1h nmr and epr spectroscopies to paral ... | 1993 | 8251511 |
| crystallographic structure of a photoreceptor protein at 2.4 a resolution. | the first essential step in protein photoreception is the capture and storage of energy from a photon. we have recently identified and isolated, from the purple photoautotrophic bacterium, ectothiorhodospira halophila, a 13,000-dalton photoactive yellow protein (pyp) that has a photocycle with kinetics similar to sensory rhodopsin and a very high quantum efficiency. to study the structural chemistry of protein photoreception, we determined, refined, and analyzed the crystallographic structure of ... | 1989 | 2771940 |
| plasmid from photosynthetic bacterium ectothiorhodospira sp. carries a transposable streptomycin resistance gene. | centrifugation through a cesium chloride density gradient and agarose gel electrophoresis of the dna from the purple non-sulfur photosynthetic bacterium ectothiorhodospira sp. resolved a single extrachromosomal element, plasmid pdg1. its size was estimated to be 13.2 kilobases by restriction endonuclease mapping. plasmid pdg1 and two restriction fragments thereof were cloned in escherichia coli c600 with plasmid pbr327 as a vector to form mixed plasmids pdgbr1, pdgbr2, and pdgbr3. the resistance ... | 1990 | 2171005 |
| primary structure of a photoactive yellow protein from the phototrophic bacterium ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore. | the complete amino acid sequence of the 125-residue photoactive yellow protein (pyp) from ectothiorhodospira halophila has been determined to be mehvafgsedientlakmddgqldglafgaiqldgdgnilqynaaegditgrdpkevigknffkdvap+ ++ ctdspefygkfkegvasgnlntmfeytfdyqmtptkvkvhmkkalsgdsywvfvkrv. this is the first sequence to be reported for this class of proteins. there is no obvious sequence homology to any other protein, although the crystal structure, known at 2.4 a resolution (mcree, d.e., et al., 1989, proc. n ... | 1993 | 8358295 |
| soluble cytochromes and a photoactive yellow protein isolated from the moderately halophilic purple phototrophic bacterium, rhodospirillum salexigens. | three soluble cytochromes were found in two strains of the halophilic non-sulfur purple bacterium rhodospirillum salexigens. these are cytochromes c2, c and c-551. cytochrome c2 was recognized by the presence of positive charge at the site of electron transfer (measured by laser flash photolysis), although the protein has an overall negative charge (pi = 4.7). cytochrome c2 has a high redox potential (300 mv) and is monomeric (13 kda). cytochrome c was recognized from its characteristic absorpti ... | 1990 | 2158819 |
| abundance, subunit composition, redox properties, and catalytic activity of the cytochrome bc1 complex from alkaliphilic and halophilic, photosynthetic members of the family ectothiorhodospiraceae. | ubiquinol-cytochrome c oxidoreductase (cytochrome bc1) complexes were demonstrated to be present in the membranes of the alkaliphilic and halophilic purple sulfur bacteria ectothiorhodospira halophila, ectothiorhodospira mobilis, and ectothiorhodospira shaposhnikovii by protoheme extraction, immunoblotting, and electron paramagnetic resonance spectroscopy. the gy values of the rieske [2fe-2s] clusters observed in membranes of e. mobilis and e. halophila were 1.895 and 1.910, respectively. in e. ... | 1993 | 8383662 |
| isolation and structure determination of a novel compatible solute from the moderately halophilic purple sulfur bacterium ectothiorhodospira marismortui. | the halophilic phototrophic bacterium ectothiorhodospira marismortui produces three organic osmolytes to counterbalance the osmotic pressure of the surrounding medium: glycine betaine, sucrose, and a novel compound. this new compound, which accounts for approximately 30% of the cells' compatible solutes, was isolated and identified by mass spectrometry and nuclear magnetic resonance. it was characterized as n alpha-carbamoyl-l-glutamine 1-amide, an unusual amino acid derivative with no previous ... | 1991 | 2050139 |
| the molecular structure of the high potential iron-sulfur protein isolated from ectothiorhodospira halophila determined at 2.5-a resolution. | the molecular structure of a high potential iron-sulfur protein (hipip) isolated from the purple photosynthetic bacterium, ectothiorhodospira halophila strain bn9626, has been solved by x-ray diffraction analysis to a nominal resolution of 2.5 a and refined to a crystallographic r value of 18.4% including all measured x-ray data from 30.0- to 2.5-a resolution. crystals used in the investigation contained two molecules/asymmetric unit and belonged to the space group p21 with unit cell dimensions ... | 1991 | 1917989 |
| polar lipids in phototrophic bacteria of the rhodospirillaceae and chromatiaceae families. | the polar lipids of photosynthetic purple bacteria of the genera chromatium, thiocapsa, thiocystis, ectothiorhodospira, rhodopseudomonas, rhodospirillum, and rhodomicrobium were analyzed. characteristic compositions of the polar lipids were found for most of the rhodospirillaceae and chromatiaceae species. phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin were the major phospholipids in most species. phosphatidylcholine was present as a major component in all species of the genus e ... | 1982 | 7076618 |
| control of nitrogenase in a photosynthetic autotrophic bacterium, ectothiorhodospira sp. | an ectothiorhodospira species fixed nitrogen when grown as an autotroph in completely inorganic medium by using a variety of electron donors. the organism also used organic carbon sources; however, this required induction of synthesis of various enzymes, whereas the enzymes needed for autotrophic growth were synthesized constitutively. nitrogenase induction and function were inhibited by ammonium chloride. nitrogenase activity was dependent on light and inhibited by oxygen. | 1982 | 6957409 |
| [relationship between growth conditions and assimilation of acetate and bicarbonate by ectothiorhodospira shaposhnikovii]. | the cells of ectothiorhodospira shaposhnikovii grown under the anaerobic conditions in the light and in the dark under the aerobic conditions in a medium with acetate can fix considerable amounts of co2 only in the presence of light. incorporation of 14c from the labeled acetate into the cells in the dark does not depend on the presence of bicarbonate and inorganic electron donors through assimilation of 14c-acetate in the light increases significantly in the presence of bicarbonate and sulfide ... | 1980 | 7392984 |
| sodium-dependent succinate uptake in purple bacterium ectothiorhodospira shaposhnikovii. | succinate, malate and fumarate uptake in purple sulfur bacterium ectothiorhodospira shaposhnikovii,. strain 1 k msu, obligatorily depends on the presence of na+. other monovalent cations such as k+, li+, nh4+ could not replace na+. experiments with energy-depleted cells have shown that succinate uptake against its concentration gradient can be energized by artifically imposed sodium gradients (delta pna). an artificial membrane potential (inside negative) inhibited delta pna-driven succinate upt ... | 1980 | 7417432 |
| resonance raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated. | resonance raman spectra of the ground state of photoactive yellow protein (pyp), a photoactive pigment found in ectothiorhodospira halophila, have been obtained with excitation at 413.1 nm using a microspinning sample cell. the resonance raman spectra of the thioester-linked 4-hydroxycinnamyl chromophore in the protein are compared with the preresonance raman spectra of the 4-hydroxycinnamyl phenyl thioester and 4-hydroxycinnamic acid model compounds at various ph values. bands at 1568, 1542, 15 ... | 1995 | 7548018 |
| photobleaching of the photoactive yellow protein from ectothiorhodospira halophila promotes binding to lipid bilayers: evidence from surface plasmon resonance spectroscopy. | the photoactive yellow protein (pyp) from the phototrophic bacterium ectothiorhodospira halophila is a small, soluble protein that undergoes reversible photobleaching upon blue light irradiation and may function to mediate the negative phototactic response. based on previous studies of the effects of solvent viscosity and of aliphatic alcohols on pyp photokinetics, we proposed that photobleaching is concomitant with a protein conformational change that exposes a hydrophobic region on the protein ... | 1995 | 7696516 |
| photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from ectothiorhodospira halophila. | the photocycle of the photoactive yellow protein (pyp) isolated from ectothiorhodospira halophila was analyzed by flash photolysis with absorption detection at low excitation photon densities and by temperature-dependent laser-induced optoacoustic spectroscopy (lioas). the quantum yield for the bleaching recovery of pyp, assumed to be identical to that for the phototransformation of pyp (pg), to the red-shifted intermediate, pr, was phi r = 0.35 +/- 0.05, much lower than the value of 0.64 report ... | 1995 | 7756529 |
| measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from ectothiorhodospira halophila. | the photocycle of the photoactive yellow protein (pyp) from ectothiorhodospira halophila was examined by time-resolved difference absorption spectroscopy in the wavelength range of 300-600 nm. both time-gated spectra and single wavelength traces were measured. global analysis of the data established that in the time domain between 5 ns and 2 s only two intermediates are involved in the room temperature photocycle of pyp, as has been proposed before (meyer t.e., e. yakali, m. a. cusanovich, and g ... | 1994 | 7819501 |
| the xanthopsins: a new family of eubacterial blue-light photoreceptors. | photoactive yellow protein (pyp) is a photoreceptor that has been isolated from three halophilic phototrophic purple bacteria. the pyp from ectothiorhodospira halophila bn9626 is the only member for which the sequence has been reported at the dna level. here we describe the cloning and sequencing of the genes encoding the pyps from e.halophila sl-1 (type strain) and rhodospirillum salexigens. the latter protein contains, like the e.halophila pyp, the chromophore trans p-coumaric acid, as we show ... | 1996 | 8670821 |
| the porins from the halophilic species ectothiorhodospira shaposhnikovii and ectothiorhodospira vacuolata. | major outer membrane proteins with porin activity were isolated from cell envelopes of the halophilic strains ectothiorhodospira shaposhnikovii n1 and ectothiorhodospira vacuolata beta1. the porins were obtained as oligomers. they dissociated into monomers by heat or edta treatment. the molecular masses of the monomers were determined by mass spectrometry to be 39,285 and 37,160 da for e. shaposhnikovii n1 and e. vacuolata beta1, respectively. both were shown by analytical ultracentrifugation to ... | 1996 | 8703193 |
| optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals. | photoactive yellow protein (pyp), isolated from ectothiorhodospira halophila, is a water soluble, 14 kda photoreceptor protein with a fully reversible photocycle resembling that of sensory rhodopsin ii. we have established the presence of photoactivity in pyp crystals and defined the relaxation kinetics of spectroscopically distinguishable species in quantitative terms. the pyp crystal has a bright yellow color and displays pronounced anisotropic absorption properties. linear dichroism measureme ... | 1995 | 7827046 |
| a complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: reduced hipip i from ectothiorhodospira halophila. | we have accounted for the effect of paramagnetism on the intensities of noes in a 73-residue paramagnetic metalloprotein, the reduced high-potential iron sulfur protein iso i from ectothiorhodospira halophila, whose solution structure had been recently solved by us. the paramagnetic effects were dealt with through a suitably modified complete relaxation matrix approach. we have then recalculated the structure through a distance geometry program by minimizing the difference between the sixth root ... | 1996 | 8820483 |
| hyperexpression of a synthetic gene encoding a high potential iron sulfur protein. | a gene encoding high potential iron sulfur protein (hipip) iso-1 from ectothiorhodospira halophila was constructed in one step from long synthetic oligonucleotides. the gene was inserted into a phagemid vector from which the hipip was expressed as a fusion protein to > 10% of the soluble protein in escherichia coli, demonstrating that a 4fe-4s protein can be highly expressed in e. coli. the recombinant hipip was purified to apparent homogeneity by affinity chromatography followed by proteolytic ... | 1994 | 7831286 |
| photobiology of bacteria. | the field of photobiology is concerned with the interactions between light and living matter. for bacteria this interaction serves three recognisable physiological functions: provision of energy, protection against excess radiation and signalling (for motility and gene expression). the chemical structure of the primary light-absorbing components in biology (the chromophores of photoactive proteins) is surprisingly simple: tetrapyrroles, polyenes and derivatised aromats are the most abundant ones ... | 1994 | 7832590 |
| amino acid sequences of cytochromes c2 and c' from the moderately halophilic purple phototrophic bacterium rhodospirillum salexigens. | rhodospirillum salexigens is a moderately halophilic purple phototrophic bacterium which grows optimally in 8% nacl. the amino acid sequences of the two principal soluble cytochromes c have been determined. one of these is a cytochrome c2, similar in size to mitochondrial cytochrome c. while clearly of the same sequence class as mitochondrial cytochrome c and the proteins from several other gram-negative bacteria, it does not show particular affinity to any already known sequence in terms of the ... | 1994 | 7893810 |
| ectothiorhodospira halophila ferrocytochrome c551: solution structure and comparison with bacterial cytochromes c. | the solution structure of the ectothiorhodospira halophila ferrocytochrome c551 has been determined. this molecule belongs to a separate class of small bacterial cytochromes c for which no 3d structure has been reported so far. it is characterized by a very low redox potential (58 mv) and is isolated from the periplasm of halophilic purple phototrophic bacteria. for the 78 residue protein, 1445 noe derived distance constraints were used in a combined simulated annealing/restrained molecular dyna ... | 1996 | 8969306 |
| functional expression and site-directed mutagenesis of photoactive yellow protein. | the gene encoding photoactive yellow protein (pyp) was isolated from ectothiorhodospira halophila, and a high-level expression system for pyp was constructed in escherichia coli. the molecular weight and the absorption spectrum of pyp expressed in e. coli were identical with those of the native pyp isolated from e. halophila. the amino acid residues which might interact with the chromophore (tyr42, glu46, thr50, arg52, and cys69) were mutated by site-directed mutagenesis and the absorption spect ... | 1997 | 9192728 |
| porin from the halophilic species ectothiorhodospira vacuolata: cloning, structure of the gene and comparison with other porins. | the gene coding for the anion-specific porin of the halophilic eubacterium ectothiorhodospira (ect.) vacuolata was cloned and sequenced, the first such gene so analyzed from a purple sulfur bacterium. it encodes a precursor protein consisting of 374 amino acid (aa)-residues including a signal peptide of 22-aa residues. comparison with aa sequences of porins from several other members of the proteobacteria revealed little homology. only two regions showed local homology with the previously sequen ... | 1997 | 9218724 |
| effect of hydration on the structure, dynamics and function of photosynthetic membranes of purple bacteria. | nmr spectra and relaxation times t1 and t2 for 31p in membranes of rhodobacter sphaeroides were investigated at different relative humidity levels. the results are compared to the hydration curves, fatty acid composition and the structure-dynamic and functional characteristics of the membranes of photosynthetic bacteria rb. sphaeroides, rhodospirillum rubrum and ectothiorhodospira shaposhnikovii. the differences in the state of lipid phase of these membranes are revealed under low humidity, and ... | 1997 | 9257278 |
| sequence-specific assignment of the 1h and 15n nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein i from ectothiorhodospira halophila. | a 1h and 15n nmr investigation through two-dimensional and three-dimensional spectroscopy has been performed on the reduced form ([fe4s4]2+) of the recombinant high-potential iron-sulfur protein (hipip) i from ectothiorhodospira halophila expressed in escherichia coli. [fe4s4]2+ clusters in proteins are paramagnetic with a relatively low mu eff of about 0.8 mu b/iron ion, but the paramagnetic effects on nuclear relaxation are so strong as to yield t1 values of a few milliseconds and linewidths o ... | 1994 | 7957186 |
| sequence, chromophore extraction and 3-d model of the photoactive yellow protein from rhodobacter sphaeroides. | the photoactive yellow protein (pyp) gene has been isolated from rhodobacter sphaeroides by probing with a homologous pcr-product. a sequence analysis shows that this pyp gene encodes a 124 aa protein with 48% identity to the three known pyps. downstream from pyp, a number of adjacent open reading frames were identified, including a gene encoding a coa-ligase homologue (pcl). this latter protein is proposed to be involved in pyp chromophore activation, required for attachment to the apoprotein. ... | 1998 | 9630474 |
| the three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein i from ectothiorhodospira halophila through nuclear magnetic resonance. | the three-dimensional structure in solution of reduced recombinant high-potential iron-sulfur protein iso-i from ectothiorhodospira halophila was determined using 948 relevant interproton noes out of the 1246 observed noes. the determination was accomplished using the xeasy program for spectral analysis and the distance geometry (dg) program diana for generation of the structure as described by wüthrich [wüthrich, k. (1989) acc. chem. res. 22, 36-44]. the fes cluster was simulated using an amino ... | 1994 | 7957187 |
| complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. | the unique ability of photoactive proteins to capture and use energy from a photon of light depends on the chromophore, its linkage to the protein, and the surrounding protein environment. to understand the molecular mechanisms by which a chromophore and protein interact to undergo a light cycle, we are studying photoactive yellow protein (pyp), a 14-kda water-soluble photoreceptor from ectothiorhodospira halophila with a photocycle similar to that of sensory rhodopsin. here, we report the cloni ... | 1994 | 7981196 |
| the photoactive yellow protein from ectothiorhodospira halophila as studied with a highly specific polyclonal antiserum: (intra)cellular localization, regulation of expression, and taxonomic distribution of cross-reacting proteins. | a rabbit antiserum was raised against the photoactive yellow protein (pyp) from ectothiorhodospira halophila and purified by adsorption experiments to obtain a highly specific polyclonal antiserum. this antiserum was used to obtain the following results. (i) in e. halophila, pyp can be isolated from the fraction of soluble proteins. in the intact cell, however, pyp appeared to be associated with (intra)cytoplasmic membranes, as was concluded from analysis of immunogold-labelled thin sections of ... | 1994 | 8021174 |
| molecular structure of the oxidized high-potential iron-sulfur protein isolated from ectothiorhodospira vacuolata. | the high-potential iron-sulfur protein (iso-form ii) isolated from ectothiorhodospira vacuolata has been crystallized and its three-dimensional structure determined by molecular replacement procedures and refined to 1.8-a resolution with a crystallographic r factor of 16.3%. crystals employed in the investigation belonged to the space group c222(1) with unit cell dimensions of a = 58.4 a, b = 64.7 a, and c = 39.3 a and one molecule per asymmetric unit. like those hipips structurally characterize ... | 1994 | 8117708 |
| amino acid sequences of cytochromes c-551 from the halophilic purple phototrophic bacteria, ectothiorhodospira halophila and e. halochloris. | the cytochromes c-551 from ectothiorhodospira halophila and e. halochloris contain 78 and 79 residues, respectively. the sequences can be aligned without the need to postulate any internal deletions or insertions to give 63% identity. they are apparently distantly related to the class i cytochromes c, based on the location of the heme attachment site near the n-terminus and the sixth ligand methionine near the c-terminus. alignment with cytochromes c5 from azotobacter and pseudomonas, with cytoc ... | 1993 | 8215425 |