| thermodynamic parameters of cytochrome c3-ferredoxin complex formation. | the complex formation between cytochrome c3 and ferredoxin i from desulfovibrio desulfuricans norway was studied by microcalorimetric and ph-stat titration measurements. the stoichiometry of the complex was found to be one molecule of cytochrome c3 per monomer of ferredoxin i. the association constant determined at t = 283 k in tris(hydroxymethyl)aminomethane hydrochloride (tris-hcl) buffer, 10(-2) m and ph 7.7, was ka = 1.3 x 10(6) m-1. though the enthalpy (delta h = 19 +/- 1 kj.mol-1) and the ... | 1987 | 2827754 |
| metabolic diversity among the dissimilatory sulfate-reducing bacteria. albert jan kluyver memorial lecture. | | 1989 | 2679377 |
| the relationship between activity and the axial g = 2.06 epr signal induced by co in the periplasmic (fe) hydrogenase from desulfovibrio vulgaris. | the effect of exposure to carbon monoxide on the activity of the (fe) hydrogenase from desulfovibrio vulgaris has been determined. concentrations of carbon monoxide which completely inhibit hydrogenase activity and induce formation of the axial g = 2.06 epr signal up to 0.8 spin/molecule do not cause irreversible inhibition of the (fe) hydrogenase. | 1988 | 2830138 |
| purification of vibrio fischeri nitrite reductase and its characterization as a hexaheme c-type cytochrome. | dissimilatory nitrite reductase was isolated from anaerobically nitrate-grown vibrio fischeri cells and purified to electrophoretic homogeneity. the enzyme catalyzes the six-electron reduction of nitrite to ammonia. upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under either nonreducing or reducing conditions, the purified nitrite reductase migrated as a single protein band of mr 57,000. gel filtration chromatography revealed a native molecular weight of 58,000, indicating the e ... | 1988 | 2833168 |
| a hypothetical model of the flavodoxin-tetraheme cytochrome c3 complex of sulfate-reducing bacteria. | a hypothetical model of the flavodoxin-tetraheme cytochrome c3 electron-transfer complex from the sulfate-reducing bacterium desulfovibrio vulgaris has been constructed by using interactive computer graphics based on electrostatic potential field calculations and previous nmr experiments. features of the proposed complex are (1) van der waals contact between the flavin mononucleotide prosthetic group of flavodoxin and one heme of the cytochrome, (2) unique complementarity of electrostatic fields ... | 1988 | 2838073 |
| assignment of individual heme epr signals of desulfovibrio baculatus (strain 9974) tetraheme cytochrome c3. a redox equilibria study. | an epr redox titration was performed on the tetraheme cytochrome c3 isolated from desulfovibrio baculatus (strain 9974), a sulfate-reducer. using spectral differences at different poised redox states of the protein, it was possible to individualize the epr g-values of each of the four hemes and also to determine the mid-point redox potentials of each individual heme: heme 4 (-70 mv) at gmax = 2.93, gmed = 2.26 and gmin = 1.51; heme 3 (-280 mv) at gmax = 3.41; heme 2 (-300 mv) at gmax = 3.05, gme ... | 1988 | 2843371 |
| cloning of genes encoding redox proteins of known amino acid sequence from a library of the desulfovibrio vulgaris (hildenborough) genome. | a library of 900 recombinant phages has been constructed for the genome of desulfovibrio vulgaris hildenborough (1.7 x 10(6) bp) by cloning size-fractionated sau3a fragments (15-20 kb) into the replacement vector lambda-2001. when a hydrogenase gene probe, a 4.7-kb sali-ecori fragment of known nucleotide sequence, was used to screen the plaque lifted library, 23 positive clones were found, which together span 31 kb of d. vulgaris dna. to facilitate the cloning of genes with oligodeoxynucleotides ... | 1988 | 2843442 |
| epr determination of interaction redox potentials in a multiheme cytochrome: cytochrome c3 from desulfovibrio desulfuricans norway. | in cytochromes c3 which contain four hemes per molecule, the redox properties of each heme may depend upon the redox state of the others. this effect can be described in terms of interaction redox potentials between the hemes and must be taken into account in the characterization of the redox properties of the molecule. we present here a method of measurement of these interactions based on the epr study of the redox equilibria of the protein. the microscopic and macroscopic midpoint potentials a ... | 1988 | 2846296 |
| purification and properties of the membrane-associated coenzyme f420-reducing hydrogenase from methanobacterium formicicum. | the membrane-associated coenzyme f420-reducing hydrogenase of methanobacterium formicicum was purified 87-fold to electrophoretic homogeneity. the enzyme contained alpha, beta, and gamma subunits (molecular weights of 43,000, 36,700, and 28,800, respectively) and formed aggregates (molecular weight, 1,020,000) of a coenzyme f420-active alpha 1 beta 1 gamma 1 trimer (molecular weight, 109,000). the hydrogenase contained 1 mol of flavin adenine dinucleotide (fad), 1 mol of nickel, 12 to 14 mol of ... | 1989 | 2738024 |
| epr-detectable redox centers of the periplasmic hydrogenase from desulfovibrio vulgaris. | the periplasmic hydrogenase of desulfovibrio vulgaris (hildenbourough ncib 8303) belongs to the category of [fe] hydrogenase which contains only iron-sulfur clusters as its prosthetic groups. amino acid analyses were performed on the purified d. vulgaris hydrogenase. the amino acid composition obtained compared very well with the result derived from the nucleotide sequence of the structural gene (voordouw, g., brenner, s. (1985) eur. j. biochem. 148, 515-520). detailed epr reductive titration st ... | 1988 | 2848804 |
| cloning and sequencing of the gene encoding cytochrome c3 from desulfovibrio vulgaris (hildenborough). | the gene encoding the redox protein cytochrome c3 from desulfovibrio vulgaris (hildenborough) has been cloned using two synthetic oligonucleotides (one 17-mer and one 18-mer), designed to recognize the structural gene. plasmid pcyc3 was derived from the clone and contains a 7.5 x 10(3)-base ecori-hindiii insert of d. vulgaris dna in puc9. a 674-base-pair fragment of this insert was sequenced with the dideoxy-chain-termination procedure and found to contain the entire structural gene encoding cyt ... | 1986 | 3019687 |
| characterization of the soluble hydrogenase from desulfovibrio africanus. | the soluble hydrogenase from desulfovibrio africanus has been isolated and characterized. the enzyme consists of two subunits of 65 kda and 27 kda. its absorption spectrum is typical of an iron-sulfur protein. the protein contains 12 iron atoms, 10 labile sulfur atoms and 0.9 nickel atom per molecule. d. africanus hydrogenase is rapidly activated under reducing conditions and exhibits a specific activity of 570 mumoles h2 evolved/min/mg. the epr spectrum of the oxidized enzyme shows no ni(iii) s ... | 1986 | 3021136 |
| characterization and complete amino acid sequence of ferredoxin ii from desulfovibrio vulgaris miyazaki. | one of 2 ferredoxins, fd ii, purified from desulfovibrio vulgaris miyazaki (dvm) has been characterized and its complete amino acid sequence established. fd ii is composed of 63 amino acid residues and contains 7 cysteinyl residues but has only 4 iron atoms in an iron-sulfur cluster of a standard redox potential of -405 mv. the arrangement of cysteinyl residues in the protein suggests that some cysteinyl residues are not directly involved in ligation to the iron-sulfur cluster. homology is recog ... | 1988 | 2855025 |
| experimental evidence of an alpha helix in desulfovibrio desulfuricans norway ferredoxin i: a two-dimensional nmr study. | desulfovibrio ferredoxins are small proteins involved in biological oxido-reduction reactions and contain either one or two (4fe-4s) clusters. the conformation of d. desulfuricans norway ferredoxin i in solution was studied by two-dimensional nmr and various conformational parameters (n.o.e. and j-coupling) indicate the presence of an alpha-helix involving residues 41 to 50. these data confirm an earlier proposal (fukuyama et al, j. mol. biol. 199, 183 (1988] in which the space of the missing cl ... | 1989 | 2930532 |
| light induced h2 evolution in a hydrogenase-tio2 particle system by direct electron transfer or via rhodium complexes. | three different hydrogenases (isolated from clostridium pasteurianum, desulfovibrio desulfuricans strain norway 4 and d. baculatus 9974) added to a suspension of tio2 (anatase) powder are able to catalyze h2 evolution under band gap illumination of the semiconducting particles, and in the presence of edta or methanol as electron donor. this h2 production can be obtained by the direct electron transfer from the conduction band of the tio2 particles to the active site of the enzyme at phs higher t ... | 1986 | 3089310 |
| analysis of the active center of hydrogenase from desulfovibrio vulgaris miyazaki by magnetic measurements. | hydrogenase [hydrogen: ferricytochrome c3 oxidoreductase, ec 1.12.2.1] solubilized and purified from the particulate fraction of desulfovibrio vulgaris miyazaki f (iam 12604) contains 8 iron and 8 labile sulfide ions in one molecule which is composed of two unequal subunits (mr: 60,000 + 29,000). it does not contain nickel atoms. the epr (electron paramagnetic resonance) spectrum has an isotropic signal at g = 2.017 which is independent of the temperature. the peak-to-peak width of the signal is ... | 1985 | 2987196 |
| electron paramagnetic resonance studies on the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from desulfovibrio gigas. | desulfovibrio gigas hydrogenase (ec 1.12.2.1) is a complex enzyme containing one nickel, one 3fe, and two [fe4s4] clusters (teixeira, m., moura, i., xavier, a. v., der vartanian, d. v., legall, j., peck, h. d., jr., huynh, b. h., and moura, j. j. g. (1983) eur. j. biochem. 130, 481-484). this hydrogenase belongs to a class of enzymes that are inactive "as isolated" (the so-called "oxygen-stable hydrogenases") and must go through an activation process in order to express full activity. the state ... | 1985 | 2991227 |
| preliminary 1h-nmr studies of the interaction between cytochrome c3 and ferredoxin i from desulfovibrio desulfuricans norway. | the complex formation of two electron transfer proteins, cytochrome c3 and ferredoxin i from desulfovibrio desulfuricans norway, has been shown by 1h-nmr spectroscopy. presence of ferredoxin i produces ferricytochrome c3 1h-nmr spectrum modifications. the chemical shift of perturbated heme methyl resonances has been used to determine the stoichiometry of the complex. at ph 7.6 and 20 degrees c, the two proteins were found to form a complex 1:1 with an association constant, ka, of 10(4) m-1. two ... | 1985 | 2992500 |
| purification and properties of thiosulfate reductase from desulfovibrio vulgaris, miyazaki f. | thiosulfate reductase was purified to an almost homogeneous state from desulfovibrio vulgaris, strain miyazaki f, by ammonium sulfate precipitation, chromatography on deae-toyopearl, ultrogel aca 34, and hydroxylapatite, and disc electrophoresis. the specific activity was increased 580-fold over the crude extract. the molecular weight was determined by gel filtration to be 85,000-89,000, differing from those reported for thiosulfate reductases from other desulfovibrio strains. the enzyme had no ... | 1985 | 2993256 |
| occurrence of sulphate-reducing bacteria in human faeces and the relationship of dissimilatory sulphate reduction to methanogenesis in the large gut. | sulphate-reducing bacteria (srb) were enumerated in 40 faecal samples obtained from two different human populations in the united kingdom and rural south africa. species able to metabolize acetate, lactate, propionate, butyrate, h2/co2, succinate, pyruvate, valerate, ethanol and a glutamate/serine/alanine mixture were found in faeces from both populations. although a variety of nutritionally and morphologically distinct species of srb belonging to the genera desulfotomaculum, desulfobacter, desu ... | 1988 | 3204069 |
| [evolution of sulfate respiration and cytochrome]. | | 1985 | 2999878 |
| cloning the ddei restriction-modification system using a two-step method. | ddei, a type ii restriction-modification system from the gram-negative anaerobic bacterium desulfovibrio desulfuricans, recognizes the sequence ctnag. the system has been cloned into e. coli in two steps. first the methylase gene was cloned into pbr322 and a derivative expressing higher levels was constructed. then the endonuclease gene was located by southern blot analyses; bamhi fragments large enough to contain the gene were cloned into pacyc184, introduced into a host containing the methylas ... | 1986 | 3022241 |
| purification of a hexaheme cytochrome c552 from escherichia coli k 12 and its properties as a nitrite reductase. | anaerobic cytochrome c552 was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration from a mutant of escherichia coli k 12 that synthesizes an increased amount of this pigment. several molecular and enzymatic properties of the cytochrome were investigated. its relative molecular mass was determined to be 69 000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. it was found to be an acidic protein that existed in the monomeric form in the native sta ... | 1986 | 3002798 |
| isolation of fumarate reductase from desulfovibrio multispirans, a sulfate reducing bacterium. | fumarate reductase was isolated and purified 100-fold to homogeneity from desulfovibrio multispirans, a new species of sulfate-reducing bacteria. the enzyme contained 1 mol of non-covalently bound fad and four subunits with mr 45,000, 32,000, 30,000 and 27,000. epr spectroscopy showed the existence of two iron-sulfur clusters. the absorption spectrum showed a broad region of high absorbance from 450 nm to 300 nm with a protein peak at 278 nm. the ratio of a278:a400 was 2.60. the specific activit ... | 1986 | 3008734 |
| application of hydrogenase for photoinduced hydrogen evolution. | various attempts have been made to develop suitable redox systems for the photochemical utilization of solar energy. recent work has shown that the three component systems containing a photosensitizer, an electron donor, and an electron acceptor can be used to evolve hydrogen when a suitable catalyst is present. the reactions are quite general and have been demonstrated for a wide range of photosensitizers and electron carriers. hydrogenase or colloidal platinum are widely used as catalysts, for ... | 1986 | 3015245 |
| activation and active sites of nickel-containing hydrogenases. | hydrogenases that contain nickel and iron-sulphur clusters also have a regulatory mechanism, by which exposure to oxidants such as oxygen prevents their reaction with hydrogen. treatment with reducing agents then causes reactivation. in some hydrogenases from desulfovibrio species, there is evidence that there are at least two different deactivated states, which differ in their rates of reductive reactivation. the membrane-bound hydrogenase of d. desulfuricans, norway strain, the periplasmic hyd ... | 1986 | 3015251 |
| hydrogenase activity in aged, nonviable desulfovibrio vulgaris cultures and its significance in anaerobic biocorrosion. | batch cultures of desulfovibrio vulgaris stored at 32 degrees c for 10 months have been found to retain 50% of the hydrogenase activity of a 1-day culture. the hydrogenase found in old cultures needs reducing conditions for its activation. viable cell counts are negative after 6 months, showing that the hydrogenase activity does not depend on the presence of viable cells. these observations are of importance in the understanding of anaerobic biocorrosion of metals caused by depolarization phenom ... | 1987 | 3310883 |
| pyruvate dehydrogenase and the path of lactate degradation in desulfovibrio vulgaris miyazaki f. | pyruvate dehydrogenase from desulfovibrio vulgaris miyazaki f was partially purified from the soluble fraction of the bacterial sonicate, and characterized. the enzyme catalyzes oxidative decarboxylation of pyruvate to produce acetyl-coa, in contrast to statements in current review articles in which acetyl phosphate is indicated to be a direct decomposition product of pyruvate in sulfate-reducing bacteria. the established reaction stoichiometry is: pyruvate + coa + fmn----acetyl-coa + co2 + fmnh ... | 1986 | 3023304 |
| preliminary x-ray studies of the tetra-heme cytochrome c3 and the octa-heme cytochrome c3 from desulfovibrio gigas. | a tetra-heme and an octa-heme cytochrome c3 from the sulfate bacterium desulfovibrio gigas have been crystallized. diffraction quality crystals of the tetra-heme cytochrome are obtained from solution by the addition of polyethylene glycol at ph 6.5. the crystals are orthorhombic, space group p2(1)2(1)2 with unit cell parameters a = 42.27 a, b = 52.54 a and c = 52.83 a. the octa-heme cytochrome crystals develop from low ionic strength solutions of phosphate or tris-cl in the ph range 6.2-7.6. the ... | 1986 | 3025018 |
| on the active sites of the [nife] hydrogenase from desulfovibrio gigas. mössbauer and redox-titration studies. | the [nife] hydrogenase isolated from desulfovibrio gigas was poised at different redox potentials and studied by mössbauer spectroscopy. the data firmly establish that this hydrogenase contains four prosthetic groups: one nickel center, one [3fe-xs], and two [4fe-4s] clusters. in the native enzyme, both the nickel and the [3fe-xs] cluster are epr-active. at low temperature (4.2 k), the [3fe-xs] cluster exhibits a paramagnetic mössbauer spectrum typical for oxidized [3fe-xs] clusters. at higher t ... | 1987 | 3027068 |
| low-spin sulfite reductases: a new homologous group of non-heme iron-siroheme proteins in anaerobic bacteria. | two new low molecular weight proteins with sulfite reductase activity, isolated from methanosarcina barkeri (dsm 800) and desulfuromonas acetoxidans (strain 5071), were studied by epr and optical spectroscopic techniques. both proteins have visible spectra similar to that of the low-spin sulfite reductase of desulfovibrio vulgaris strain hildenborough and no band at 715 nm, characteristic of high-spin fe3+ complexes in isobacteriochlorins is observed. epr shows that as isolated the siroheme is i ... | 1986 | 3028382 |
| purification and characterization of desulfovibrio vulgaris (hildenborough) hydrogenase expressed in escherichia coli. | hydrogenase from desulfovibrio vulgaris (hildenborough) is a heterologous dimer of molecular mass 46 + 13.5 kda. its two structural genes have been cloned on a 4664-base-pair fragment of known sequence in the vector puc9. expression of hydrogenase polypeptides in escherichia coli transformed with this plasmid is poor (approximately 0.1% w/w of total protein). deletion of up to 1.9 kb of insert dna brings the gene encoding for the large subunit in close proximity to the lac promotor of puc9 and r ... | 1987 | 3028789 |
| rubredoxin from desulfovibrio gigas. a molecular model of the oxidized form at 1.4 a resolution. | the crystal structure of rubredoxin from the sulfate-reducing bacterium desulfovibrio gigas has been determined at 1.4 a resolution (1 a = 0.1 nm) by x-ray diffraction methods; starting with a model of the isostructural rubredoxin from desulfovibrio vulgaris. refinement of the molecular model has been carried out by restrained least-squares techniques and fourier series calculations. the present model includes a formyl at the n-terminal end and 121 possible sites for solvent molecules with full ... | 1987 | 3441010 |
| the evolution of prokaryotic ferredoxins--with a general method correcting for unobserved substitutions in less branched lineages. | thirty-one bacterial type ferredoxins were examined by means of the parsimony method for their phylogenetic implications. the results show reasonable relationships in that photosynthetic, thermophilic, and desulfovibrio groups are identifiable; but a number of interesting anomalies occur. these include a methanogen sequence that clusters among the desulfovibrios. there are several differences from the phylogeny of woese. at least two duplications producing paralogous genes are demonstrated, plus ... | 1987 | 3447013 |
| characterization of the cytochrome system of a nitrogen-fixing strain of a sulfate-reducing bacterium: desulfovibrio desulfuricans strain berre-eau. | two c-type cytochromes were purified and characterized by electron paramagnetic resonance (epr) and nuclear magnetic resonance (nmr) spectroscopic techniques, from the sulfate-reducer nitrogen-fixing organism, desulfovibrio desulfuricans strain berre-eau (ncib 8387). the purification procedures included several chromatographic steps on alumina, carboxymethylcellulose and gel filtration. a tetrahaem and a monohaem cytochrome were identified. the multihaem cytochrome has visible, epr and nmr spect ... | 1987 | 3030740 |
| putative signal peptide on the small subunit of the periplasmic hydrogenase from desulfovibrio vulgaris. | we sequenced the nh2 terminus of the large and small subunits of the periplasmic hydrogenase from the sulfate-reducing bacterium desulfovibrio vulgaris (hildenborough) and found that the small subunit lacks a region of 34 nh4-terminal amino acids coded by the gene for the small subunit (g. voordouw and s. brenner, eur. j. biochem. 148:515-520, 1985). we suggest that this region constitutes a signal peptide based on comparison with known procaryotic signal peptides. | 1986 | 3525521 |
| cloning in escherichia coli of genes involved in the synthesis of proline and leucine in desulfovibrio desulfuricans norway. | a library of desulfovibrio desulfuricans norway genomic dna was constructed in escherichia coli with pbr322 as vector and plasmids able to complement the proa and leub mutations of the host were screened. it was observed that all the plasmids studied were highly unstable, the insert dna being rapidly lost under non-selective growth conditions. a 2.75 kb dna fragment of d. desulfuricans norway was found to complement e. coli proa, prob and proc deficiencies. from the results of restriction analys ... | 1987 | 3033436 |
| aerobic degradation of choline by proteus mirabilis: enzymatic requirements and pathway. | cleavage of choline to trimethylamine and acetaldehyde by extracts of proteus mirabilis requires both particulate and soluble protein fractions, k+, and a bound divalent metal cation. the reaction shows a long lag period, abolished only by preincubation of the particulate fraction in the complete reaction system. the two-carbon fragment produced is acetaldehyde; choline cleavage appears to be tightly coupled to dismutation of the acetaldehyde to ethanol and acetate, as indicated by stimulation b ... | 1986 | 3536045 |
| direct electron transfer reactions of cytochrome c553 from desulfovibrio vulgaris hildenborough at indium oxide electrodes. | the direct, heterogeneous, electron transfer reactions of cytochrome c553 from desulfovibrio vulgaris hildenborough have been studied at indium oxide optically transparent electrodes. these reactions have been studied using cyclic voltammetry and derivative cyclic voltabsorptometry and the kinetics of heterogeneous electron transfer is quasi-reversible. the thermodynamics and kinetics of electron transfer by this molecule can be studied at this electrode surface without the need for surface modi ... | 1987 | 3036137 |
| model of a complex between the tetrahemic cytochrome c3 and the ferredoxin i from desulfovibrio desulfuricans (norway strain). | a three-dimensional model of an electron-transfer complex between the tetrahemic cytochrome c3 and the ferredoxin i from the sulfate-reducing bacterium desulfovibrio desulfuricans (norway strain) has been generated through computer graphics methods. the model is based on the known x-ray structure of the cytochrome and on a model of the ferredoxin that has been derived through computer graphics modeling and energy minimization methods, from the x-ray structure of the homologous ferredoxin from pe ... | 1988 | 2847143 |
| nucleotide sequence of the genetic loci encoding subunits of bradyrhizobium japonicum uptake hydrogenase. | an indispensable part of the hydrogen-recycling system in bradyrhizobium japonicum is the uptake hydrogenase, which is composed of 34.5- and 65.9-kda subunits. the gene encoding the large subunit is located on a 5.9-kilobase fragment of the h2-uptake-complementing cosmid phu52 [zuber, m., harker, a.r., sultana, m.a. & evans, h.j. (1986) proc. natl. acad. sci. usa 83, 7668-7672]. we have now determined that the structural genes for both subunits are present on this fragment. two open reading fram ... | 1988 | 3054886 |
| cloning and sequencing of the genes encoding the large and the small subunits of the h2 uptake hydrogenase (hup) of rhodobacter capsulatus. | the structural genes (hup) of the h2 uptake hydrogenase of rhodobacter capsulatus were isolated from a cosmid gene library of r. capsulatus dna by hybridization of bradyrhizobium japonicum. the r. capsulatus genes were localized on a 3.5 kb hindiii fragment. the fragment, cloned onto plasmid pac76, restored hydrogenase activity and autotrophic growth of the r. capsulatus mutant jp91, deficient in hydrogenase activity (hup-). the nucleotide sequence, determined by the dideoxy chain termination me ... | 1988 | 3067084 |
| the three classes of hydrogenases from sulfate-reducing bacteria of the genus desulfovibrio. | three types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus desulfovibrio. they differ in their subunit and metal compositions, physico-chemical characteristics, amino acid sequences, immunological reactivities, gene structures and their catalytic properties. broadly, the hydrogenases can be considered as 'iron only' hydrogenases and nickel-containing hydrogenases. the iron-sulfur-containing hydrogenase ([fe] hydrogenase) contains two ferredoxin-type (4fe-4s) c ... | 1988 | 3078655 |
| differential inhibition of catalytic sites in desulfovibrio gigas hydrogenase. | the hydrogenase of desulfovibrio gigas has been shown to contain one nickel atom, a cluster with three irons and two clusters of the [4fe-4s] type in an 89 kda molecule. though evidence that the nickel ion is involved in the site of hydrogen activation has been presented for this and other hydrogenases, the role of nickel and of the other redox centres in the protein remains to be firmly identified. we have examined the effects of inhibitors of hydrogenase activity in an attempt to identify the ... | 1986 | 3089313 |
| isolation, amino acid analysis and n-terminal sequence determination of the two subunits of the nickel-containing hydrogenase of desulfovibrio gigas. | the two subunits of the nickel-iron hydrogenase from desulfovibrio gigas have been purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and their amino acid compositions have been determined. the n-terminal sequences for 15 residues of the large subunit (mr 62,000) and 25 residues of the small subunit (mr 26,000), respectively, were established. the occurrence of several cysteine residues in the small subunit is discussed in relation with their possible role in the b ... | 1988 | 3134950 |
| cloning, nucleotide sequence, and expression of the flavodoxin gene from desulfovibrio vulgaris (hildenborough). | the gene coding for the flavodoxin protein from desulfovibrio vulgaris (hildenborough) has been identified, cloned, and sequenced. dna fragments containing the flavodoxin gene were identified by hybridization of a mixed synthetic heptadecanucleotide probe to southern blots of sali-digested genomic dna. the nucleotide sequences of the probe were derived from the published protein primary structure (dubourdieu, m., legall, j., and fox, j. l. (1973) biochem. biophys. res. commun. 52, 1418-1425). th ... | 1988 | 3170590 |
| a comparative carbon-13, nitrogen-15, and phosphorus-31 nuclear magnetic resonance study on the flavodoxins from clostridium mp, megasphaera elsdenii, and azotobacter vinelandii. | the flavodoxins from megasphaera elsdenii, clostridium mp, and azotobacter vinelandii were studied by 13c, 15n, and 31p nmr techniques by using various selectivity enriched oxidized riboflavin 5'-phosphate (fmn) derivatives. it is shown that the pi electron distribution in protein-bound flavin differs from that of free flavin and depends also on the apoflavoprotein used. in the oxidized state clostridium mp and m. elsdenii flavodoxins are very similar with respect to specific hydrogen bond inter ... | 1986 | 3801391 |
| amino acid sequence of ferredoxin i from desulfovibrio vulgaris miyazaki. | the amino acid sequence of ferredoxin (fd) i, purified from desulfovibrio vulgaris miyazaki, has been established. fd i is strikingly similar to fd iii of d. africanus benghazi with 84% homology. both have the sequence, -cys-x-x-asp-x-x-cys-x-x-x-cys-pro- in the n-terminal half, and the sequence, -cys-x-x-cys-x-x-cys-x-x-x-cys-glu- in the c-terminal half of the molecule, instead of the common sequences for ligation to the usual [4fe-4s] clusters. fd i has 76% homology to fd ii of d. desulfurican ... | 1988 | 3182762 |
| use of a three-stage continuous culture system to study the effect of mucin on dissimilatory sulfate reduction and methanogenesis by mixed populations of human gut bacteria. | a mixed culture of human fecal bacteria was grown for 120 days in a three-stage continuous culture system. to reproduce some of the nutritional and ph characteristics of the large gut, each vessel had a different operating volume (0.3, 0.5, and 0.8 liter) and ph (6.0, 6.5, and 7.0). a mixture of polysaccharides and proteins was used as carbon and nitrogen sources. measurements of h2, ch4, s2-, sulfate reduction rates, sulfate-reducing bacteria (srb), and volatile fatty acids were made throughout ... | 1988 | 3214155 |
| crystallization and preliminary x-ray diffraction study of a protein with a high potential rubredoxin center and a hemerythrin-type fe center. | a newly discovered iron-containing protein, isolated from the bacterium desulfovibrio vulgaris (hildenborough, ncib 8303), has been crystallized. the molecule appears to be a dimer of mass 44kda. this protein has iron centers with spectrascopic similarities to those in rubredoxins and in hemerythrins. the x-ray diffraction shows symmetry consistent with space group i222 or i212121. cell parameters are a = 49.2 a, b = 81.3 a, c = 100.1 a, and alpha, beta, gamma = 90 degrees. x-ray diffraction dat ... | 1988 | 3255104 |
| electron transfer between the hydrogenase from desulfovibrio vulgaris (hildenborough) and viologens. 1. investigations by cyclic voltammetry. | the electron transfer kinetics between the hydrogenase from desulvovibrio vulgaris (strain hildenborough) and three different viologen mediators has been investigated by cyclic voltammetry. the mediators methyl viologen, di(n-aminopropyl) viologen and propyl viologen sulfonate differ in redox potential and in net charge. dependent on the ph both the one- and two-electron-reduced forms or only the two-electron-reduced form of the viologens are effective in electron exchange with hydrogenase. calc ... | 1988 | 3289919 |
| electron transfer between the hydrogenase from desulfovibrio vulgaris (hildenborough) and viologens. 2. investigations by chronoamperometry. | the electron transfer kinetics between the hydrogenase from desulfovibrio vulgaris (strain hildenborough) and the mediators methyl viologen, di-(n-aminopropyl) viologen and propyl viologen sulfonate have been investigated by chronoamperometry. second-order rate constants were calculated on basis of the theory for a simple catalytic mechanism and are compared with the results obtained before by cyclic voltammetry (preceding paper in this journal). from the ionic-strength dependence and the observ ... | 1988 | 3289920 |
| the base sequence of the niff gene of klebsiella pneumoniae and homology of the predicted amino acid sequence of its protein product to other flavodoxins. | the nucleotide sequence of a 629 base-pair segment of dna spanning the niff gene of klebsiella pneumoniae is presented. the structural gene comprises 531 base-pairs (175 codons, excluding the translational initiator and terminator) encoding an acidic polypeptide of 18950 da. the niff product thus belongs to the long-chain class of flavodoxins. it shows some sequence homology to the short-chain flavodoxins from desulfovibrio vulgaris, clostridium mp and megasphaera elsdenii, and much stronger hom ... | 1985 | 3911951 |
| reversible activation of hydrogenase from escherichia coli. | hydrogenase from escherichia coli exhibited low activity when assayed for hydrogen:methyl viologen reductase activity and no activity when assayed for hydrogen-uptake activity with acceptors of high redox potential (dichloroindophenol, methylene blue). nor did the enzyme as isolated catalyse proton-tritium exchange activity. incubation under hydrogen resulted in an increase in hydrogen-uptake activity with methyl viologen and the appearance of hydrogen-uptake activity with dichloroindophenol and ... | 1987 | 3297695 |
| new perspectives on bacterial ferredoxin evolution. | recent evidence indicates that a gene transposition event occurred during the evolution of the bacterial ferredoxins subsequent to the ancestral intrasequence gene duplication. in light of this new information, the relationships among the bacterial ferredoxins were reexamined and an evolutionary tree consistent with this new understanding was derived. the bacterial ferredoxins can be divided into several groups based on their sequence properties; these include the clostridial-type ferredoxins, t ... | 1985 | 3932661 |
| crystallization, preliminary x-ray study and crystal activity of the hydrogenase from desulfovibrio gigas. | hydrogenase (ec 1.12) from desulfovibrio gigas is a dimeric enzyme (26 and 62 (x 10(3) mr) that catalyzes the reversible oxidation of molecular hydrogen. single crystals of hydrogenase have been produced using the hanging drop method, with either peg (polyethylene glycol) 6000 or ammonium sulfate as precipitants at ph 6.5. x-ray examination of the crystals indicates that those obtained with ammonium sulfate are suitable for structure determination to at least 3.0 a resolution when synchrotron ra ... | 1987 | 3309347 |
| cloning and sequencing of the genes encoding the large and small subunits of the periplasmic (nifese) hydrogenase of desulfovibrio baculatus. | the genes coding for the large and small subunits of the periplasmic hydrogenase from desulfovibrio baculatus have been cloned and sequenced. the genes are arranged in an operon with the small subunit gene preceding the large subunit gene. the small subunit gene codes for a 32 amino acid leader sequence supporting the periplasmic localization of the protein, however no ferredoxin-like or other characteristic iron-sulfur coordination sites were observed. the periplasmic hydrogenases from d. bacul ... | 1987 | 3316183 |
| uncommonly encountered, motile, anaerobic gram-negative bacilli associated with infection. | motile, anaerobic gram-negative bacilli belonging to the genera butyrivibrio, succinimonas, succinivibrio, anaerovibrio, wolinella, campylobacter, desulfovibrio, selenomonas, and anaerobiospirillum are being recognized in clinical specimens with increasing frequency. over a 12.5-year period at the va wadsworth medical center, 13 clinical specimens yielded one of these organisms. six isolates were recovered from infected wounds, five from respiratory tract specimens obtained from patients with an ... | 1987 | 3321364 |
| identification of three classes of hydrogenase in the genus, desulfovibrio. | a comparison of amino-terminal amino acid sequences from the large and small subunits of hydrogenases from desulfovibrio reveals significant differences. these results, in conjunction with antibody analyses, clearly indicate that the iron, iron + nickel, and iron + nickel + selenium containing hydrogenases represent three distinct classes of hydrogenase in desulfovibrio. | 1987 | 3322275 |
| cloning, characterization, and sequencing of the genes encoding the large and small subunits of the periplasmic [nife]hydrogenase of desulfovibrio gigas. | the structural genes for the large and small subunits of desulfovibrio gigas periplasmic [nife]hydrogenase were identified and isolated by immunological and oligonucleotide screening. the gene for the small subunit codes for a 266-amino-acid, 28,724-dalton polypeptide which is separated by 63 nucleotides from the large subunit gene that codes for a 560-amino-acid, 61,707-dalton polypeptide. a putative signal peptide precedes the small subunit coding region, which may direct transport of the enzy ... | 1987 | 3322743 |
| fine structural observations of desulfovibrio desulfuricans. | | 1973 | 4123231 |
| morphology of bacteriophage-like particles from desulfovibrio vulgaris. | phagelike particles obtained from a mitomycin c-induced lysate of desulfovibrio vulgaris are described. whether they can be classified as temperate bacteriophages or as bacteriocins has not been determined. | 1973 | 4125584 |
| on the role of menaquinone-6 in the electron transport of hydrogen: fumarate reductase system in the strict anaerobe desulfovibrio gigas. | | 1974 | 4132528 |
| contamination of chrome-tanned leather by desulfovibrio. | | 1966 | 4161880 |
| n-terminal amino acid sequences of azotobacter vinelandii and rhodospirillum rubrum flavodoxins. | | 1974 | 4212186 |
| dinitrophenol-stimulated adenosine triphosphatase activity in extracts of desulfovibrio gigas. | a dinitrophenol (dnp)-stimulated adenosine triphosphatase (atpase) has been found in both the soluble and particulate fractions of the anaerobic sulfate-reducing bacterium, desulfovibrio gigas. as the soluble atpase was labile to storage, only the particulate enzyme was studied in detail. it was optimally stimulated by dnp at 4 mm, and activity was insensitive to inhibition by ouabain. the atpase was stimulated by both ca(2+) and mg(2+), but the magnitude of the stimulation was dependent upon ph ... | 1971 | 4254119 |
| purification and properties of l-alanine dehydrogenase from desulfovibrio desulfuricans. | the l-alanine dehydrogenase from cell-free extracts of desulfovibrio desulfuricans was purified approximately 56-fold. the michaelis constants for the substrates of the amination reaction and the ph optima for the reactions catalyzed by this enzyme closely agree with those reported for other l-alanine dehydrogenases. pyruvate was found to inhibit the amination reaction. the enzyme was absolutely specific for l-alanine and nicotinamide adenine dinucleotide. its sensitivity to para-chloromecuriben ... | 1968 | 4298732 |
| [photochemical and enzymatic reduction of flavodoxin isolated from desulfovibrio gigas]. | | 1968 | 4302850 |
| rubredoxin from a nitrogen-fixing variety of desulfovibrio desulfuricans. | | 1968 | 4303402 |
| menadione reductase from desulfovibrio gigas. | | 1970 | 4318157 |
| homology of ribosomal ribonucleic acid of desulfovibrio species with desulfovibrio vulgaris. | three species of desulfovibrio were found to have a high degree of ribosomal ribonucleic acid homology with desulfovibrio vulgaris. desulfotomaculum nigrificans, which is also a sulfate-reducing anaerobe, had only 38% ribosomal ribonucleic acid homology with d. vulgaris. the homologies of six other unrelated genera were determined and found to be lower than 50%. | 1971 | 4326740 |
| electron paramagnetic resonance and light absorption studies on c-type cytochromes of the anaerobic sulfate reducer desulfovibrio. | | 1971 | 4330153 |
| evidence for the involvement of non-heme iron in the active site of hydrogenase from desulfovibrio vulgaris. | | 1971 | 4330154 |
| electron paramagnetic resonance studies on the reaction of exogenous ligands with cytochrome c 3 from desulfovibrio vulgaris. | | 1971 | 4330631 |
| the bacterial nitrate reductases: epr studies on nitrate reductase a from micrococcus denitrificans. | | 1972 | 4335844 |
| electrophoretic characterization of atp-sulfate adenylytransferase (atp-sulfurylase) using acrylamide gels. | | 1972 | 4339369 |
| biochemical studies on sulfate-reducing bacteria. xii. some properties of flavodoxin from desulfovibrio vulgaris. | | 1973 | 4350899 |
| kinetic studies on hydrogenase. parahydrogen-orthohydrogen conversion and hydrogen-deuterium exchange reactions. | | 1973 | 4352847 |
| an iron tetrahydroporphyrin prosthetic group common to both assimilatory and dissimilatory sulfite reductases. | | 1973 | 4354952 |
| amino acid sequence of cytochrome c3 from desulfovibrio vulgaris. | | 1974 | 4358550 |
| a monomolecular electron transfer chain: structure and function of cytochrome c3. | | 1974 | 4364940 |
| proton magnetic resonance studies of desulfovibrio cytochromes c3. | | 1974 | 4365252 |
| biochemical studies on sulfate-ruducing bacteria. 8. sulfite reductase from desulfovibrio vulgaris--mechanism of trithionate, thiosulfate, and sulfide formation and enzymatic properties. | | 1974 | 4365884 |
| outline structure of cytochrome c3 and consideration of its properties. | | 1974 | 4365942 |
| [partial purification and study of nad:rubredoxin oxidoreductase from d. gigas]. | | 1968 | 4384975 |
| [study of the metabolism of dicarboxylic acids and of pyruvate in sulfo-reducing bacteria. i. study of the enzyme oxidation of fumarate in acetate]. | | 1970 | 4392009 |
| reduction of alkyl hydroperoxides to alcohols: role of rubredoxin, an electron carrier in the bacterial hydroxylation of hydrocarbons. | | 1971 | 4399432 |
| on the mechanism of adenylyl sulfate reductase for the sulfate-reducing bacterium, desulfovibrio vulgaris. | | 1972 | 4405088 |
| flavodoxin from the sulfate reducing bacterium desulfovibrio vulgaris. its structure at 2.5 a resolution. | | 1972 | 4405091 |
| temperature-jump studies of desulfovibrio vulgaris flavodoxin: kinetics of fmn binding and of reduction of semiquinone by methyl viologen. | | 1974 | 4420157 |
| observations on the bisulfite reductase (p582) isolated from desulfotomaculum nigrificans. | the bisulfite reductase (p582) from desulfotomaculum nigrificans was purified to homogeneity as judged by polyacrylamide gel electrophoresis. by colorimetric methods of analysis, the products of bisulfite reduction by this enzyme were determined to be trithionate, thiosulfate, and sulfide. of these, trithionate was consistently found to be the major product, whereas the latter two were formed in lesser quantities. when [(35)s]bisulfite was incorporated as substrate, no labeled sulfide was detect ... | 1974 | 4424068 |
| purification and characterization of ferredoxin from desulfovibrio vulgaris miyazaki. | two ferredoxins, fd i and fd ii, were isolated and purified from desulfovibrio vulgaris miyazaki. the major component, fd i, is an iron-sulfur protein of mr 12,000, composed of two identical subunits. the absorption spectra of fd i and fd ii have a broad absorption shoulder near 400 nm characteristic of iron-sulfur proteins. the purity index, a400/a280, of fd i is 0.69, and its millimolar absorption coefficient at 400 nm is 3.73 per fe. it contains two redox centers with discrete redox behaviors ... | 1988 | 3360752 |
| [a new non-spore forming thermophilic organism, reducing sulfates, desulfovibrio thermophilus nov. sp]. | | 1974 | 4449494 |
| rapid electrocatalytic procedure for hydrogenase kinetic determination in the h2 evolution direction. | the linear sweep voltammetric method is used as a new approach for kinetic determination with enzymes accepting reversible redox couples as cosubstrate. a monolayer of hydrogenase molecules is grafted onto a glassy carbon electrode which is both the support of the enzyme and the detector of the activity. reduced viologen concentration in the enzyme microenvironment is controlled by the electrode potential. the catalytic current produced by the enzyme allows an easy kinetic constant determination ... | 1986 | 3516152 |
| sulfate reduction by a desulfovibrio species isolated from sheep rumen. | several dissimilatory, sulfate-reducing bacteria were isolated from the rumen fluid of sheep fed purified diets containing sulfate. one isolate, strain d, was selected for characterization. this organism is a nonsporeforming, obligately anaerobic, mesophilic, nonmotile, gram-negative, straight rod. cell-free extracts show absorption maxima for cytochrome c(3) and desulfoviridin, characteristic of desulfovibrio. carbohydrates, as a sole carbon source, will support growth. lactate supports growth ... | 1974 | 4472525 |
| structure of the oxidized form of a flavodoxin at 2.5-angstrom resolution: resolution of the phase ambiguity by anomalous scattering. | flavodoxin from desulfovibrio vulgaris crystallizes in the oxidized form as well-formed, tetragonal bipyramids, space group p4(3)2(1)2, unit-cell parameters, a = b = 51.6 a, c = 139.6 a, 8 molecules per unit cell. the structure has been determined at 2.5-a resolution with phases based on a single isomorphous derivative. the phase ambiguity of a single derivative was resolved by use of anomalous scattering from the single-site sm(+3). the molecule has a five-strand pleated sheet core with two lon ... | 1972 | 4508313 |
| structure of the radical form of clostridial flavodoxin: a new molecular model. | interpretation of a new electron-density map at 3.25-a resolution has led to a somewhat revised model for the free radical (semiquinone) structure of flavodoxin from clostridium mp. although the general conformation of the molecule is very similar to that of oxidized desulfovibrio vulgaris flavodoxin, flavin mononucleotide-protein interactions are not identical in the two flavodoxins. in the cl. mp semiquinone molecule, the isoalloxazine ring appears to retain the essentially planar conformation ... | 1972 | 4508314 |
| the binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0-angstrom resolution. | the crystal structure of the oxidized form of flavodoxin from desulfovibrio vulgaris has been studied at 2.0-a resolution, and a detailed description of the region around the flavin mononucleotide binding site is now available. the flavin is between a tyrosine group, roughly parallel to it on one side, and a tryptophan, about 45 degrees from being parallel, on the other side. the two carbonyl groups and two nitrogen atoms of the flavin are hydrogen bonded to the peptide chain of the protein, whi ... | 1973 | 4521211 |
| redox potentials of certain vitamins k: implications for a role in sulfite reduction by obligately anaerobic bacteria. | redox potentials of a menaquinone (mk-6), isolated in earlier researches from two species of the obligately anaerobic genus, desulfovibrio, as well as two other vitamins k(2)-menaquinones (mk-5) and (mk-9)- have been determined polarographically. the measurements have been validated by determination of redox potentials of 1,4-naphthoquinone and vitamin k(1) which agree with published potentiometric values. e(m7) for menaquinone (mk-6) is -0.067 +/- 0.010 v. redox potentials calculated for termin ... | 1974 | 4521797 |
| [microbiological preparation of mud substances used in pelotherapy]. | | 1972 | 4538492 |