| thiosulfate reductase of desulfovibrio vulgaris. | the thiosulfate reductase of desulfovibrio vulgaris has been purified and some of its properties have been determined. only one protein component was detected when the purified enzyme was subjected to polyacrylamide gel electrophoresis at ph values of 8.9, 8.0, and 7.6. in the presence of h(2), the enzyme, when coupled to hydrogenase and with methyl viologen as an electron carrier, catalyzed the reduction of thiosulfate to hydogen sulfide. the use of specifically labeled (35)s-thiosulfate reveal ... | 1971 | 5573735 |
| isolation from aspergillus nidulans, of a protein catalyzing the reduction of sulfite by reduced viologen dyes. | | 1967 | 5589532 |
| purification and properties of hydrogenases of different origins. | | 1968 | 5650411 |
| the stereospecificity of the citrate synthase in sulfate-reducing and photosynthetic bacteria. | | 1968 | 5680354 |
| the amino acid sequence of cytochrome c3 from desulfovibrio vulgaris. (n.c. i.b. 8303). | | 1968 | 5685884 |
| a note on the production of radioactive sulphide by desulfovibrio desulfuricans. | | 1968 | 5702041 |
| spontaneous spheroplast formation by desulfovibrio aestuarii. | | 1968 | 5710267 |
| [serological study of sulfate reducing bacteria (genus desulfovibrio) isolated in rumania]. | | 1968 | 5754602 |
| intermediary formation of trithionate in sulfite reduction by a sulfate-reducing bacterium. | | 1969 | 5771706 |
| a non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans. | | 1969 | 5773435 |
| amino acid composition of ferredoxin and rubredoxin isolated from desulfovibrio gigas. | the composition of ferredoxin and rubredoxin from desulfovibrio gigas was determined. ferrodoxin contained five cysteines, two methionines, and four irons. the rubredoxin was not unique. | 1969 | 5781581 |
| hydrogenase measurement with photochemically reduced methyl viologen. | methyl viologen was reduced photochemically in the presence of proflavine and ethylenediaminetetraacetic acid. the reduced methyl viologen was oxidized by hydrogenase from vibrio succinogenes. h(2) and oxidized methyl viologen were the products. hydrogenase activity was determined by spectrophotometric measurement of the disappearance of reduced methyl viologen at 600 nm. the extinction coefficient of reduced methyl viologen was determined and is 8.25 mm(-1) x cm(-1) at 600 nm. optimal condition ... | 1969 | 5781586 |
| thiosulfate reductase isolated from desulfotomaculum nigrificans. | a thiosulfate reductase from desulfotomaculum nigrificans has been partially purified by ammonium sulfate fractionation, diethylaminoethylcellulose chromatography, and sucrose density gradient centrifugation. with inner-and outer-labeled (35)s-thiosulfate, the enzyme reduced only the outer sulfur atom to hydrogen sulfide. the enzyme was inhibited by sulfite and also by several sulfhydryl inhibitors. the k(m) value for this enzyme was calculated to be 1.3 x 10(-1)m. other inorganic sulfur compoun ... | 1969 | 5784203 |
| methane as a minor product of pyruvic phosphooclasm in desulfovibrio. | | 1969 | 5795908 |
| evidence for thiosulfate formation during sulfite reduction by desulfovibrio vulgaris. | | 1969 | 5799644 |
| role of ferredoxin in the synthesis of alpha-ketobutyrate from propionyl coenzyme a and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria. | | 1969 | 5800441 |
| formation of thiosulfate from sulfite by desulfovibrio vulgaris. | crude extracts of desulfovibrio vulgaris reduced sulfite to sulfide. ammonium sulfate fractionation of crude extracts separated a thiosulfate-forming system from sulfite- and thiosulfate-reductase activities. further purification by sucrose density centrifugation separated the thiosulfate-forming system into two components, both of which were required for the reaction. in addition to these two components, cytochrome c(3), ferredoxin, and hydrogenase were required to form thiosulfate from sulfite ... | 1969 | 5802606 |
| classification of the spore-forming sulfate-reducing bacteria. | | 1965 | 5826606 |
| base composition of deoxyribonucleic acid of sulfate-reducing bacteria deduced from buoyant density measurements in cesium chloride. | saunders, grady f. (university of illinois, urbana), l. leon campbell, and john r. postgate. base composition of deoxyribonucleic acid of sulfate-reducing bacteria deduced from buoyant density measurements in cesium chloride. j. bacteriol. 87:1073-1078. 1964.-the base composition of the deoxyribonucleic acid (dna) of sulfate-reducing bacteria was calculated from buoyant density measurements in cscl. the sporulating sulfate-reducing bacteria fell into two groups: desulfovibrio orientis with a dna ... | 1964 | 5874533 |
| [study on bacterial alginolysis in marine media]. | | 1966 | 5908538 |
| media for sulphur bacteria. | | 1966 | 5924318 |
| desulfovibrio africans sp. n., a new dissimilatory sulfate-reducing bacterium. | campbell, l. leon (university of illinois, urbana), mary a. kasprzycki, and john r. postgate. desulfovibrio africanus sp. n., a new dissimilatory sulfate-reducing bacterium. j. bacteriol. 92:1122-1127. 1966.-the strains benghazi and walvis bay can be distinguished from 40 strains of desulfovibrio and from d. gigas on the basis of morphological and immunological studies. electron microscopy revealed polar lophotrichous flagellation similar to that of d. gigas but different from the characteristic ... | 1966 | 5927208 |
| purification of acetokinase from desulfovibrio desulfuricans. | | 1966 | 5927210 |
| dependance of sulfite reduction on a crystallized ferredoxin from desulfovibrio gigas. | | 1966 | 5928906 |
| growth of desulfovibrio desulfuricans under heterotrophic and anaerobic conditions. | alico, robert k. (st. bonaventure university, st. bonaventure, n.y.), and francis w. liegey. growth of desulfovibrio desulfuricans, under heterotrophic and anaerobic conditions. j. bacteriol. 91:1112-1114. 1966.-growth of desulfovibrio desulfuricans was investigated under heterotrophic and anaerobic conditions. for initial growth to occur, it was found that the e(h) or redox potential must be at least 0 mv. some carbon sources were tested, and those which could be metabolized by d. desulfuricans ... | 1966 | 5929745 |
| phosphorylation coupled with electron transfer in extracts of the sulfate reducing bacterium, desulfovibrio gigas. | | 1966 | 5937326 |
| the electron carrier specificities of the hydrogenases of different origins. | | 1966 | 5937337 |
| pyruvate-carbon dioxide exchange reaction of desulfovibrio desulfuricans. | suh, byungse (university of kansas, lawrence), and j. m. akagi. pyruvate-carbon dioxide exchange reaction of desulfovibrio desulfuricans. j. bacteriol. 91:2281-2285. 1966.-the pyruvate-co(2) exchange reaction, catalyzed by desulfovibrio desulfuricans, required the presence of phosphate and coenzyme a. however, the requirement for phosphate disappeared when the concentration of coenzyme a was increased to a level of 3.8 x 10(-3)m. passing crude extracts through a diethylaminoethyl-cellulose colum ... | 1966 | 5943942 |
| growth of sulphate-reducing bacteria by fumarate dismutation. | | 1966 | 5953822 |
| growth of desulfovibrio on the surface of agar media. | growth of desulfovibrio desulfuricans (api strain) was found to take place in an atmosphere of hydrogen on the agar surface of complex media, including yeast extract (difco), and trypticase soy agar (bbl) without any added reducing agents. for growth on a 2% yeast extract-agar surface in the absence of hydrogen (nitrogen atmosphere), sodium lactate was required in the medium. growth on the surface of trypticase soy agar (tsa) under nitrogen took place readily in the absence of an added hydrogen ... | 1966 | 5955798 |
| role of carbon dioxide and acetate in biosynthesis by sulphate-reducing bacteria. | | 1966 | 5960530 |
| infrared spectra of some sulphate-reducing bacteria. | | 1966 | 5965362 |
| [carbon and energy sources of biosynthesis in sulfate reducing bacteria]. | | 1966 | 6002773 |
| [study on constructive metabolism of sulphate reducing bacteria using c-14]. | | 1966 | 6003015 |
| disulfur monoxide: production by desulfovibrio. | desulfovibrio desulfuricans growing on agar surfaces produces a gas that appears to be identical to "schenk's sulfur monoxide," which was later identified as disulfur monoxide the gas stimulates surface growth of desulfovibrio on an agar medium and is used by the cells as an electron donor for the reduction of benzyl viologen. | 1967 | 6024190 |
| electron carries for the phosphoroclastic reaction of desulfovibrio desulfuricans. | | 1967 | 6026239 |
| presence and stereospecificity of citrate synthase in anaerobic bacteria. | | 1967 | 6032450 |
| stimulation of the phosphoroclastic system of desulfovibrio by nucleotide triphosphates. | | 1967 | 6049364 |
| [biochemical comparison of type c3 bacterial cytochromes]. | | 1967 | 6056738 |
| biological nitrogen fixation. | | 1967 | 6067409 |
| the genomes of desulfovibrio gigas and d. vulgaris. | two-dimensional electrophoresis of sequential double-restriction digests showed that the genome of desulfovibrio gigas compromised 1.63 x 10(6) bp (1.09 x 10(9) dal) of dna; an ammonia-limited chemostat population possessed an average of nine genomes per cell and a multiplying batch culture possessed approximately 17 genomes per cell. the genome size of d. vulgaris (hildenborough) was 1.72 x 10(6) bp (1.14 x 10(9) dal); a population from an ammonia-limited batch culture contained four genomes pe ... | 1984 | 6088669 |
| characterization of cytochrome c3 from the thermophilic sulfate reducer thermodesulfobacterium commune. | a c3 type cytochrome has been purified from the thermophilic, non-spore-forming, sulfate-reducing bacterium thermodesulfobacterium commune. the purified protein was homogeneous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration, and isoelectric focusing. a pi of 6.83 was observed. the molecular weight of the cytochrome was estimated to be ca. 13,000 from both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. the hemoprotein exhibite ... | 1984 | 6090384 |
| hydrogenase, electron-transfer proteins, and energy coupling in the sulfate-reducing bacteria desulfovibrio. | | 1984 | 6093686 |
| a study of the oxidized form of pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism. | the magnetic properties at different temperatures of oxidized pseudomonas aeruginosa cytochrome c-551 peroxidase were studied, with the use of the technique of magnetic-circular-dichroism spectroscopy. at 4.2k, both constituent haems were found to be low-spin, and the axial ligand pairs were identified as histidine-histidine and histidine-methionine. at room temperature high-spin signals were observed, amounting to less than 25% of the total haem present. these signals are concluded to arise mai ... | 1984 | 6093773 |
| spectral and kinetic abnormality during the reduction of cytochrome c3 catalyzed by hydrogenase with hydrogen. | reduction process of cytochrome c3 by hydrogenase (ec 1.12.2.1) under h2 was analyzed by means of spectrophotometry. when cytochrome c3 is in equilibrium with h2 under reduced pressure, spectral abnormality in the soret region appeared most significantly in 1/4 reduction state, less significantly at 1/2 reduction state, and disappeared at 3/4 reduction state. the spectral changes during the enzymic reduction of cytochrome c3 in h2-saturated solution traced at several wavelengths also showed spec ... | 1984 | 6093872 |
| purification and properties of the soluble hydrogenase from desulfovibrio desulfuricans (strain norway 4). | a soluble hydrogenase has been isolated from desulfovibrio desulfuricans (strain norway 4) grown on postgate's medium. the enzyme differs significantly from a membrane-bound hydrogenase previously purified from the same organism grown on starkey's medium. the enzyme consisted of two subunits of 56 kda and 29 kda compared with masses of 60 kda and 27 kda for the membrane-bound enzyme. analysis of preparations of the soluble enzyme by various methods gave values of 5-10 iron atoms, 6 labile sulphu ... | 1984 | 6096145 |
| spectroscopic studies of the nature of the iron clusters in the soluble hydrogenase from desulfovibrio desulfuricans (strain norway 4). | 57fe-enriched samples of the soluble hydrogenase from desulfovibrio desulfuricans (norway) have been investigated in both the native (oxidized) and the dithionite-reduced states using mössbauer spectroscopy. the data clearly show that the iron in this enzyme is predominantly in the form of iron-sulphur clusters which are closely similar to the [4fe-4s] clusters found in a large number of ferredoxins, such as that from bacillus stearothermophilus. there appear to be two [4fe-4s] clusters. the iro ... | 1984 | 6096146 |
| characterization of a sulfite reductase from desulfovibrio vulgaris. evidence for the presence of a low-spin siroheme and an exchange-coupled siroheme-[4fe-4s] unit. | we have studied a low-molecular-weight (mr = 27,200) sulfite reductase from desulfovibrio vulgaris (hildenborough, ncib 8303) with mössbauer, epr, and chemical techniques. this sulfite reductase was found to contain one siroheme and one [4fe-4s] cluster. as purified, the siroheme is low-spin ferric (s = 1/2) which exhibits characteristic epr resonances at g = 2.44, 2.36, and 1.77. at 150 k, the observed mössbauer parameters, delta eq = 2.49 +/- 0.02 mm/s and delta = 0.31 +/- 0.02 mm/s, for the s ... | 1984 | 6096368 |
| a cytoplasmic nickel-iron hydrogenase with high specific activity from desulfovibrio multispirans sp. n., a new species of sulfate reducing bacterium. | a hydrogenase from a new species of sulfate reducing bacterium has been isolated and characterized. in contrast to other hydrogenases isolated from desulfovibrio, this enzyme is found in the cytoplasmic fraction rather than in the periplasm. the specific activity of the enzyme, as measured in the hydrogen evolution assay, is twice as high as the specific activity of the hydrogenase from d. gigas. it also differentiates itself from the periplasmic desulfovibrio hydrogenases by being more active i ... | 1984 | 6097250 |
| comparative bioenergetics of sulfate reduction in desulfovibrio and desulfotomaculum spp. | extracts of desulfotomaculum nigrificans, desulfotomaculum orientis, and desulfotomaculum ruminis exhibit low levels of inorganic pyrophosphatase but were found to have high levels of pyrophosphate:acetate phosphotransferase. conversely, extracts of desulfovibrio gigas, desulfovibrio vulgaris, and desulfovibrio desulfuricans norway 4 were shown to have high levels of inorganic pyrophosphatase but negligible amounts of pyrophosphate:acetate phosphotransferase. both enzymes are reductant activated ... | 1981 | 6109714 |
| biochemistry of dissimilatory sulphate reduction. | extensive information is available on the enzymology of respiratory sulphate reduction and the structure of electron transfer proteins isolated from the sulphate-reducing bacteria; however, it has not yet been possible to delineate satisfactorily the function of these electron transfer proteins in terms of the enzymes involved in respiratory sulphate reduction. new information about differences in pyrophosphate metabolism by desulfovibrio and desulfotomaculum, cellular localizations of electron ... | 1982 | 6127735 |
| studies on sulfite reduction by desulfovibrio vulgaris. | dissimilatory reduction of sulfites by desulfovibrio vulgaris was investigated. medium with alpha-glycerophosphate as a source of organic carbon and phosphorus was applied. it was found that sulfite at the concentration up to 1m na2so3 is not toxic for d. vulgaris and acts efficiently as an electron acceptor. basing on the presented results, a general mechanism of microbiological transformation of sulfites is proposed. | 1981 | 6174026 |
| cytochrome c3 from the sulfate-reducing anaerobe desulfovibrio africanus benghazi: antigenic properties. | antisera were prepared against cytochromes c3 from desulfovibrio africanus, d. vulgaris, and d. salexigens. cross-reactions were observed between antisera to d. vulgaris and d. africanus cytochromes and heterologous cytochromes c3. a weak cross-reaction with antisera against both d. vulgaris and d. africanus cytochromes and the acid form of the d. salexigens cytochrome was seen; the basic form did not react. | 1982 | 6181052 |
| mössbauer and epr studies of desulforedoxin from desulfovibrio gigas. | | 1980 | 6244281 |
| a cobalt containing protein isolated from desulfovibrio gigas, a sulfate reducer. | | 1980 | 6244822 |
| evidence for a three-iron center in a ferredoxin from desulfovibrio gigas. mössbauer and epr studies. | the tetrameric form of a desulfovibrio gigas ferredoxin, named fd ii, mediates electron transfer between cytochrome c3 and sulfite reductase. we have studied two stable oxidation states of this protein with mössbauer spectroscopy and electron paramagnetic resonance. we found 3 iron atoms/monomer and a spin concentration of 0.9 spins/monomer for the oxidized protein. taken together, the epr and mössbauer data demonstrate conclusively the presence of a spin-coupled structure containing 3 iron atom ... | 1980 | 6245073 |
| highly active immobilized hydrogenase from desulfovibrio gigas. | | 1980 | 6245644 |
| restriction endonucleases and their recognition sequences. | | 1980 | 6249680 |
| amino acid sequence of cytochrome c3 from desulfovibrio vulgaris, miyazaki. | the complete amino acid sequence of a tetrahemoprotein, cytochrome c3 isolated from desulfovibrio vulgaris, miyazaki, was determined to be ala-pro-lys-ala-pro-ala-asp-gly-leu-lys-met-asp-lys-thr-lys-gln-pro-val-val-phe -asn-his-ser-thr-his-lys-ala-val-lys-cys-gly-asp-cys-his-his-pro-val-asn-gly-lys-glu-asn-tyr-gln-lys-cys-ala-thr-ala-gly-cys-his-asp-asn-met-asp-lys-lys-asp-lys-ser-ala-lys-gly-tyr-tyr-his-ala-met-his-asp-lys-gly-thr-lys-phe-lys-ser-cys-val-gly-cys-his-leu-glu-thr-ala-gly-ala-asp- ... | 1980 | 6249799 |
| on the nature of the oxidation-reduction properties of nitrite reductase from desulfovibrio desulfuricans. | | 1980 | 6254507 |
| a new restriction endonuclease from the anaerobic bacterium, desulfovibrio desulfuricans, norway. | the purification and characterization of a new restriction endonuclease, dde 1, from a sulfate-reducing, anaerobic bacterium, desulfovibrio desulfuricans, norway, is reported. the enzyme recognizes the sequence (see formula index) and cleaves at the position indicated by the arrows. the enzyme preparation obtained is suitable for restriction mapping an ligation. | 1980 | 6255409 |
| phospholipid biosynthesis in some anaerobic bacteria. | we have identified and characterized enzymes of phospholipid synthesis in two plasmalogen-rich anaerobes. megasphaera elsdenii and veillonella parvula, and one anaerobe lacking plasmalogens. desulfovibrio vulgaris. all three species contained phosphatidate cytidylyltransferase and phosphatidylserine synthase. phosphatidylglycerophosphate synthesis was detected only d. vulgaris extracts. phosphatidylserine (diacyl form) was the major product of the phosphatidylserine synthase assay with particles ... | 1981 | 6263870 |
| the three-iron cluster in a ferredoxin from desulphovibrio gigas. a low-temperature magnetic circular dichroism study. | ferredoxin ii from desulphovibrio gigas is a tetrameric protein containing a novel iron-sulphur cluster consisting of three iron atoms. the low-temperature magnetic circular dichroism (mcd) spectra of the oxidized and dithionite-reduced forms of ferredoxin ii have been measured over the wavelength range approx. 300-800 nm. both oxidation levels of the cluster are shown to be paramagnetic, although only the oxidized form gives an epr signal. mcd magnetization curves have been constructed over the ... | 1981 | 6268181 |
| the structure of cytochrome c3 from desulfovibrio vulgaris miyazaki at 2.5 a resolution. | the structure of tetraheme cytochrome c3 isolated from desulfovibrio vulgaris miyazaki has been determined at 2.5 a resolution by an x-ray diffraction method. protein phases were computed by the multiple isomorphous replacement method using the native and four heavy atom derivatives, anomalous scattering measurements of the latter being considered. the mean figure of merit was 0.77. four heme groups are exposed on the surface of the molecule. there are some short helical segments in the polypept ... | 1981 | 6268619 |
| on cytochrome c3 folding. | the structure of cytochrome c3 from desulfovibrio vulgaris miyazaki (dvm) is considered in detail by scrutinizing main chain folding together with the structure of the protein from d. desulfuricans norway (ddn). the relative arrangement of the four heme groups in this molecule is similar to that of ddn and the disposition of alpha-carbon atoms of cysteine and histidine residues binding to heme groups is also similar. structural differences between the two proteins occur in the shape of some spec ... | 1981 | 6277878 |
| iron-sulphur cluster composition and redox properties of two ferredoxins from desulfovibrio desulfuricans norway strain. | two ferredoxins from desulfovibrio desulfuricans, norway strain, were investigated by epr spectroscopy. ferredoxin i appears to be a conventional [4fe-4s]2+;1+ ferredoxin, with a midpoint reduction potential of -374 mv at ph 8. ferredoxin ii when reduced, at first showed a more complex spectrum, indicating an interaction between two [4fe-4s] clusters, and probably, has two clusters per protein subunit. upon reductive titration ferredoxin ii changed to give a spectrum in which no intercluster int ... | 1982 | 6279148 |
| interconversions of [3fe-3s] and [4fe-4s] clusters. mössbauer and electron paramagnetic resonance studies of desulfovibrio gigas ferredoxin ii. | | 1982 | 6281263 |
| activation, reduction and proton-deuterium exchange reaction of the periplasmic hydrogenase from desulfovibrio gigas in relation with the role of cytochrome c3. | | 1982 | 6282633 |
| purification and characterization of cytochrome c3 (mr 26,000) isolated form desulfovibrio desulfuricans norway strain. | | 1982 | 6284155 |
| the presence of redox-sensitive nickel in the periplasmic hydrogenase from desulfovibrio gigas. | | 1982 | 6285924 |
| cytochrome c553 from desulfovibrio vulgaris: potentiometric characterization by optical and epr studies. | | 1982 | 6288033 |
| ferredoxin from methanosarcina barkeri: evidence for the presence of a three-iron center. | methanosarcina barkeri ferredoxin was purified and characterized by electron paramagnetic resonance (epr) and mössbauer spectroscopy. the purification procedure included chromatographic steps on deae-cellulose and gel filtration. the isolated protein is unstable under aerobic conditions. the ferredoxin exhibits charge transfer bands at 283 nm and 405 nm with an absorption ratio a405/a283 = 0.73. its molecular weight has been estimated to be 20000-22000 by gel filtration chromatography. the nativ ... | 1982 | 6290216 |
| nmr redox studies of desulfovibrio vulgaris cytochrome c3. electron transfer mechanisms. | the 300-mhz proton nmr spectra of the tetrahaem cytochrome c3 from desulfovibrio vulgaris were examined while varying the ph and the redox potential. the analysis of the complete nmr reoxidation pattern was done taking into account all the 16 redox states that can be present in the redox titration of a tetra-redox-center molecule. a network of saturation transfer experiments performed at different oxidation stages, between the fully reduced and the fully oxidized states, allowed the observation ... | 1982 | 6291937 |
| crystal structure and electron transfer properties of cytochrome c3. | the crystal structure of cytochrome c3 from the sulfate-reducing bacteria desulfovibrio desulfuricans, norway strain, has been determined through the fitting of the recently completed primary structure to a 2.5 a resolution electron density map. the phase calculations were based on three mercurial derivatives; anomalous scattering data were used to refine the four heme iron positions. a preliminary refinement of the molecular model has led to a conventional crystallographic r factor of 34%. cyto ... | 1982 | 6292223 |
| a pulse-radiolysis study of cytochrome c3. kinetics of the reduction of cytochrome c3 by methyl viologen radicals and the characterisation of the redox properties of cytochrome c3 from desulfovibrio vulgaris (hildenborough). | 1. pulse-radiolysis experiments were performed in the presence of methyl viologen and cytochrome c3. after the pulse, methyl viologen radicals are formed and the kinetics of these radicals with cytochrome c3 are studied, the reaction between cytochrome c3 and methyl viologen radicals (mv+) is diffusion controlled. the ionic strength dependence and the ph-dependence of this reaction were studied. from the ionic strength dependence (at ph 7.8) we found that the net charge of the fully oxidized cyt ... | 1982 | 6293820 |
| evidence for nickel and a three-iron center in the hydrogenase of desulfovibrio desulfuricans. | hydrogenase from desulfovibrio desulfuricans (atcc no. 27774) grown in unenriched and in enriched 61ni and 57fe media has been purified to apparent homogeneity. two fractions of enzymes with hydrogenase activity were separated and were termed hydrogenase i and hydrogenase ii. they were shown to have similar molecular weights (77,600 for hydrogenase i and 75,500 for hydrogenase ii), to be composed of two polypeptide chains, and to contain ni and non-heme iron. because of its higher specific activ ... | 1982 | 6294073 |
| unambiguous identification of the nickel epr signal in 61ni-enriched desulfovibrio gigas hydrogenase. | | 1982 | 6295382 |
| desulfovibrio gigas hydrogenase: redox properties of the nickel and iron-sulfur centers. | below 30 k, oxidized desulfovibrio gigas hydrogenase presents an intense electron paramagnetic resonance (epr) signal centered at g = 2.02, typical of an iron-sulfur center. in addition a rhombic epr signal, attributed to ni(iii) species, is also observed [legall, j., ljungdahl, p., moura, i., peck, h.d., jr, xavier, a.v., moura, j.j.g., teixeira, m., huynh, b.h., and dervartanian, d.v. (1982) biochem. biophys. res. commun. 106, 610-616; and cammack, r., patil, d., aguirre, r., and hatchikian, e ... | 1983 | 6297907 |
| iron-sulfur stoichiometry and structure of iron-sulfur clusters in three-iron proteins: evidence for [3fe-4s] clusters. | beef heart aconitase contains 3fe clusters in its inactive and 4fe clusters in its active form. the fully active form can be restored from the inactive one by insertion of fe(2+), whereas s(2-) is not required. chemical analyses for iron and labile sulfide yield fe/s(2-) ratios of 0.66-0.74 for the inactive and 0.90-1.03 for the active form. sulfane sulfur (s(0)) was not detected. we propose on the basis of these data that the inactive form may arise from the active one by loss of one iron only ... | 1983 | 6300839 |
| purification and properties of the membrane-bound by hydrogenase from desulfovibrio desulfuricans. | the membrane-bound hydrogenase from the anaerobic sulphate-reducing bacterium desulfovibrio desulfuricans (norway strain) has been purified to homogeneity, with an overall 80-fold purification and a specific activity of 70 mumol of h2 evolved/min per mg of protein. the hydrogenase had a relative molecular mass of 58 000 as determined by gel filtration and was estimated to contain six iron atoms and six acid-labile sulphur groups per molecule. the absorption spectrum of the enzyme was characteris ... | 1983 | 6303306 |
| comparative studies of monohemic bacterial c-type cytochromes. redox and optical properties of desulfovibrio desulfuricans norway cytochrome c553(550) and pseudomonas aeruginosa cytochrome c551. | redox properties of cytochrome c553(550) from desulfovibrio desulfuricans norway (eo' = 0.04 + 0.02 v/nhe) and cytochrome c551 from p. aeruginosa (eo = 0.25 +/- 0.02 v/nhe) are compared with those of some monohemic c-type cytochromes. the pk value for the equilibrium between the ph-dependent forms of cytochrome c553(550) (pk = 10.3 +/- 0.1) has been also determined. it is to be noted that the difference between redox potentials can extend to nearly 250 mv, though the axial heme ligands are ident ... | 1983 | 6307291 |
| electron paramagnetic resonance and other properties of hydrogenases isolated from desulfovibrio vulgaris (strain hildenborough) and megasphaera elsdenii. | the hydrogenases of desulfovibrio vulgaris and megasphaera elsdenii are compared with respect to some of their physical properties. in addition to fe the only metal ions that are present in significant amounts are ni and cu. from cluster extrusion experiments it follows that the d. vulgaris enzyme contains three 4 fe-4s clusters, while m. elsdenii hydrogenase only releases part of its fe-s clusters. the resting d. vulgaris enzyme shows only a small 3 fe-xs type of epr signal (maximum 5% electron ... | 1983 | 6311546 |
| esr characteristics of sulfhydryl-containing peptide-nickel (iii) complexes: implication for nickel (iii) center of hydrogenases. | the ni(iii) complexes of n-mercaptoacetylglycyl-l-histidine and n-mercaptoacetylglycylglycylglycine clearly show the rhombic esr pattern and g-values similar to the ni(iii) chromophore of hydrogenases. the present results strongly suggest that the ni(iii) center of hydrogenases contains one cysteine sulfur coordination as equatorial ligand in a tetragonal geometry. in addition, axial nitrogen ligand and a sulfur-rich ni(iii) site as in an s4 donor set may be ruled out. indeed, the ni(iii) esr fe ... | 1983 | 6313001 |
| coordination of the heme iron in the low-potential cytochromes c-553 from desulfovibrio vulgaris and desulfovibrio desulfuricans. different chirality of the axially bound methionine in the oxidized and reduced states. | the coordination geometry at the heme iron of the cytochromes c-553 from desulfovibrio vulgaris and desulfovibrio desulfuricans was investigated by 1h-nuclear magnetic resonance and circular dichroism spectroscopy. individual assignments were obtained for heme c and the axial ligands. from studies of nuclear overhauser enhancements the axial histidine imidazole ring orientation relative to the heme group was found to coincide with other c-type cytochromes. in contrast, a new structure was observ ... | 1983 | 6313059 |
| amino acid sequence of cytochrome c-553 from desulfovibrio vulgaris miyazaki. | the complete amino acid sequence of cytochrome c-553 from desulfovibrio vulgaris miyazaki has been determined. the protein has a single polypeptide chain containing 79 amino acid residues and has the typical characteristics of small mitochondrial cytochromes. contrary to the expectation that the amino acid sequence of cytochrome c-553 from d. vulgaris miyazaki is closely related to that from d. vulgaris hildenborough, the two are not alike, except for the 20 nh2-terminal residues and the 4 carbo ... | 1983 | 6313657 |
| refined structure of cytochrome c3 at 1.8 a resolution. | the structure of cytochrome c3 from the sulfate-reducing bacterium desulfovibrio vulgaris miyazaki has been successfully refined at 1.8 a resolution. the crystallographic r factor is 0.176 for 9907 significant reflections. the isotropic temperature factors of individual atoms were refined and a total of 47 water molecules located on the difference map were incorporated in the refinement. the four heme groups are closely packed, with adjacent pairs of heme planes being nearly perpendicular to eac ... | 1984 | 6319712 |
| molybdenum exafs of the desulfovibrio gigas mo(2fe-2s) protein--structural similarity to "desulfo" xanthine dehydrogenase. | the molybdenum exafs of the mo(2fe-2s) protein from desulfovibrio gigas has been examined using fluorescence detection and synchrotron radiation. in the oxidized form the molybdenum environment is found to contain two terminal oxo groups and two long (2.47 a) mo-s bonds. evidence was also found for an oxygen or nitrogen donor ligand at 1.90 a. addition of dithionite to the oxidized enzyme results in loss of a terminal oxo group, perhaps due to protonation. in addition, a 0.1 a contraction in the ... | 1984 | 6325597 |
| application of hydrophobic chromatography to the large scale purification of desulfovibrio desulfuricans cytochrome c3. | hydrophobic chromatography on phenyl-sepharose was employed for large scale purification of cytochrome c3 from desulfovibrio desulfuricans. this chromatographic procedure minimizes operational volumes and eliminates the lengthy dialysis ordinarily used to remove large amounts of salts. pure cytochrome c3 was obtained after one additional purification by ion-exchange chromatography. | 1984 | 6326080 |
| desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous epr and mössbauer spectra. | a purification procedure for the periplasmic hydrogenase from desulfovibrio vulgaris ( hildenborough , national collection of industrial bacteria 8303) is reported. the purified hydrogenase has a specific activity of 4800 units per mg of protein. plasma emission studies reveal that this highly active hydrogenase is free of nickel and contains 11 (+/- 1) nonheme iron atoms per molecule. a combined epr and mössbauer study indicates that the majority of the iron atoms are bound in the form of iron- ... | 1984 | 6328525 |
| correlations studies between structural and redox properties of cytochromes c3. | individual redox potential values are determined for different cytochromes c3. these polyhaemic cytochromes can be divided into two groups: one characterized by only one marked reduction step, the other one giving at least two well-marked reduction steps corresponding to redox potential values ranging from - 0.120 to - 0.400 v. correlations between potential values and structural data are discussed. | 1984 | 6329165 |
| characterization of three iron ferredoxins by microwave power saturation. | we have measured the electronic spin lattice relaxation time t1 in the temperature range 4 k-10 k, by microwave power saturation on the 3fe ferredoxins from desulfovibrio gigas and azotobacter vinelandii. the comparison with the results previously obtained on other iron sulfur proteins emphasizes the particularly fast relaxing properties of the e.p.r. signal in 3fe ferredoxins. these results support the models of the active site which predict very low lying excited levels. | 1984 | 6329322 |
| electron transfer mechanism and interaction studies between cytochrome c3 and ferredoxin. | ferredoxin, cytochrome c3 and hydrogenase are specific partners of the sulfate reduction pathway of desulfovibrio desulfuricans norway and might be exemplary for electron exchange mechanism studies. cytochrome c3 contains four low redox potential haems for 13 000 molecular weight. two ferredoxins isolated from the same bacteria are dimers of 6 000 molecular weight per subunit (ferredoxin i: one (4 fe-4s) cluster per subunit, ferredoxin ii: two (4 fe-4 s) clusters per subunit). the amino acid seq ... | 1984 | 6329323 |
| nmr studies of electron transfer mechanisms in a protein with interacting redox centres: desulfovibrio gigas cytochrome c3. | the proton nmr spectra of the tetrahaem cytochrome c3 from desulfovibrio gigas were examined while varying the ph and the redox potential. the analysis of the nmr reoxidation pattern was based on a model for the electron distribution between the four haems that takes into account haem-haem redox interactions. the intramolecular electron exchange is fast on the nmr time scale (larger than 10(5) s-1). the nmr data concerning the ph dependence of the chemical shift of haem methyl resonances in diff ... | 1984 | 6329752 |
| interconversion from 3fe into 4fe clusters in the presence of desulfovibrio gigas cell extracts. | desulfovibrio gigas ferredoxin ii (fdii) contains a single 3fe cluster [huynh, b.h., moura, j.j.g., moura, i., kent, t.a., legall, j., xavier, a.v., and münck, e. (1980) j. biol. chem. 255, 3242-3244]. in the oxidized state the protein exhibits an intense electron paramagnetic resonance (epr) signal at g = 2.02. upon one-electron reduction the center becomes epr silent. in the presence of d. gigas crude cell extracts, devoid of acidic electron carriers and supplemented with pyruvate and fdii, an ... | 1984 | 6329755 |
| kinetic properties of hydrogenase isolated from desulfovibrio vulgaris (hildenborough). | hydrogenase of desulfovibrio vulgaris shows nonlinear kinetics in hydrogen production with both the natural electron carrier, cytochrome c3, and the artificial donor, methyl viologen semiquinone. increasing concentrations of salt progressively inhibit the hydrogen production, as do increasing amounts of dimethylsulfoxide (me2so). hydrogen consumption activity does not change up to 30% (v/v) of me2so. preincubation in me2so up to 55% (v/v) does not affect the hydrogen uptake or production. the pr ... | 1983 | 6339237 |
| three-iron clusters in iron-sulfur proteins. | contents. 1. introduction and history. 2. characteristic spectroscopic features of 3fe clusters. 1. general considerations. 2. mössbauer spectroscopy. 3. magnetic circular dichroism (mcd) spectroscopy. 4. electron paramagnetic resonance (epr) spectroscopy. 5. resonance raman (rr) spectroscopy. 6. extended x-ray fine-structure (exafs) spectroscopy. 3. results of x-ray diffraction studies. 4. proteins containing or showing features characteristic of 3fe clusters 1. overview. 2. ferredoxin i of azo ... | 1983 | 6342537 |
| [microbiological synthesis of tetrapyrrole compounds]. | this paper reviews publications on the biosynthesis of functional tetrapyrroles by microorganisms. emphasis is given to the structure of uroporphyrin iii methylated derivatives termed corriphyrins and their involvement in the formation of two groups of tetrapyrrole pigments--corrinoids and siroheme. current concepts concerning the final stages of the formation of the corrine ring and potential cobalt-free precursors of vitamin b12 are discussed. it is indicated that the data available may help e ... | 1983 | 6344060 |
| bidirectional measurement of hydrogenase activity by the ph-stat method. | the protons produced by the catalytic activity of hydrogenase in h2 evolution from dithionite-reduced methyl viologen or through benzyl viologen reduction by h2 gas are automatically titrated by a ph-stat device. this approach allows the measurement of hydrogenase activity and ensures the constancy of ph during the reaction in absence of buffers. kinetic assays and ph and temperature-dependence experiments with desulfovibrio gigas hydrogenase performed by this method basically confirm the result ... | 1983 | 6351666 |
| resonance raman studies of beef heart aconitase and a bacterial hydrogenase. | the resonance raman (rr) spectra of beef heart aconitase and of an air-stable hydrogenase from desulfuvibrio desulfuricans, as isolated, are characteristic of 3fe centers. activation of aconitase by fe(ii) addition converts the rr spectrum to one characteristic of [4fe-4s]2+ clusters. analytical data on aconitase, as isolated, confirms the recent finding (beinert, h., emptage, m. h., dreyer, j.-l., scott, r. a., hahn, j. e., hodgson, k. o., and thomson, a. j. (1983) proc. natl. acad. sci. u. s. ... | 1983 | 6355093 |
| immobilization of isolated and cellular hydrogenase of d. desulfuricans in radiation-polymerized polyacrylamides. | purified hydrogenase from desulfovibrio desulfuricans was immobilized either by entrapment or absorption onto porous neutral and charged acrylamide beads. surface absorption and crosslinking on the beads resulted in a high hydrogenase activity and a good immobilization coefficient compared to the enzyme and whole cells entrapped in the same matrix. maximum enzyme activity (citrate-phosphate buffer) was shifted to ph 6.5 upon immobilization in contrast to 6.0 for the free enzyme and the range of ... | 1984 | 6383215 |