| Sequential and structural analysis of [NiFe]-hydrogenase-maturation proteins from Desulfovibrio vulgaris Miyazaki F. Agrawal A.G., Voordouw G., Gartner W.
Antonie Van Leeuwenhoek 90:281-290(2006) · UniProtKB (2) |
| The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M. et al.
Nat. Biotechnol. 22:554-559(2004) · UniProtKB (3,517) |
| Hydration structures in proteins and neutron diffraction experiment on dissimilatory sul te reductase D (DsrD). Chatake T., Ostermann A., Kurihara K., Parak F.G., Mizuno N., Voordouw G., Higuchi Y., Tanaka I., Niimura N.
J Synchrotron Radiat 11:72-75(2004) · Mapped (1) |
| Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris. Chatake T., Mizuno N., Voordouw G., Higuchi Y., Arai S., Tanaka I., Niimura N.
Acta Crystallogr. D Biol. Crystallogr. 59:2306-2309(2003) · Mapped (1) |
| Crystal structure of dissimilatory sulfite reductase D (DsrD) protein--possible interaction with B- and Z-DNA by its winged-helix motif. Mizuno N., Voordouw G., Miki K., Sarai A., Higuchi Y.
Structure 11:1133-1140(2003) · Mapped (1) |
| Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin. McCarthy A.A., Walsh M.A., Verma C.S., O'Connell D.P., Reinhold M., Yalloway G.N., D'Arcy D., Higgins T.M., Voordouw G., Mayhew S.G.
Biochemistry 41:10950-10962(2002) · Mapped (1) |
| Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system. Lumppio H.L., Shenvi N.V., Summers A.O., Voordouw G., Kurtz D.M. Jr.
J. Bacteriol. 183:101-108(2001) · UniProtKB (1) |
| Deletion of the rbo gene increases the oxygen sensitivity of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Voordouw J.K., Voordouw G.
Appl. Environ. Microbiol. 64:2882-2887(1998) · UniProtKB (1) |
| Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: thermodynamic properties and crystal structures of glycine-61 mutants. O'Farrell P.A., Walsh M.A., McCarthy A.A., Higgins T.M., Voordouw G., Mayhew S.G.
Biochemistry 37:8405-8416(1998) · Mapped (1) |
| ISD1, an insertion element from the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough: structure, transposition, and distribution. Fu R., Voordouw G.
Appl. Environ. Microbiol. 64:53-61(1998) · UniProtKB (2) |
| The dcr gene family of Desulfovibrio: implications from the sequence of dcrH and phylogenetic comparison with other mcp genes. Deckers H.M., Voordouw G.
Antonie Van Leeuwenhoek 70:21-29(1996) · UniProtKB (1) |
| Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory sulfite reductase and of the alpha- and beta-subunit genes is not coordinately regulated. Karkhoff-Schweizer R.R., Bruschi M., Voordouw G.
Eur. J. Biochem. 211:501-507(1993) · UniProtKB (1) |
| The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. Rossi M., Pollock W.B.R., Reij M.W., Keon R.G., Fu R., Voordouw G.
J. Bacteriol. 175:4699-4711(1993) · UniProtKB (8) |
| Identification of a large family of genes for putative chemoreceptor proteins in an ordered library of the Desulfovibrio vulgaris Hildenborough genome. Deckers H.M., Voordouw G.
J. Bacteriol. 176:351-358(1994) · UniProtKB (11) |
| Overexpression of Desulfovibrio vulgaris Hildenborough cytochrome c553 in Desulfovibrio desulfuricans G200. Evidence of conformational heterogeneity in the oxidized protein by NMR. Blanchard L., Marion D., Pollock B., Voordouw G., Wall J., Bruschi M., Guerlesquin F.
Eur. J. Biochem. 218:293-301(1993) · UniProtKB (2) |
| Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR. Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.
Appl. Environ. Microbiol. 61:290-296(1995) · UniProtKB (4) |
| Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers. Voordouw G., van der Vies S.M., Eweg J.K., Veeger C., van Breemen J.F.L., van Bruggen E.F.J.
Eur. J. Biochem. 111:347-355(1980) · UniProtKB (1) |
| Physiochemical properties of thermomycolase, the thermostable, extracellular, serine protease of the fungus Malbranchea pulchella. Voordouw G., Gaucher G.M., Roche R.S.
Can. J. Biochem. 52:981-990(1974) · UniProtKB (1) |
| Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough). Voordouw G., Brenner S.
Eur. J. Biochem. 148:515-520(1985) · UniProtKB (3) |
| Cloning and sequencing of the gene encoding cytochrome c3 from Desulfovibrio vulgaris (Hildenborough). Voordouw G., Brenner S.
Eur. J. Biochem. 159:347-351(1986) · UniProtKB (1) |
| Cloning of genes encoding redox proteins of known amino acid sequence from a library of the Desulfovibrio vulgaris (Hildenborough) genome. Voordouw G.
Gene 67:75-83(1988) · UniProtKB (1) |
| Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello. Voordouw G., Strang J.D., Wilson F.R.
J. Bacteriol. 171:3881-3889(1989) · UniProtKB (2) |
| Analysis and comparison of nucleotide sequences encoding the genes for [NiFe] and [NiFeSe] hydrogenases from Desulfovibrio gigas and Desulfovibrio baculatus. Voordouw G., Menon N.K., le Gall J., Choi E.S., Peck H.D. Jr., Przybyla A.E.
J. Bacteriol. 171:2894-2899(1989) · UniProtKB (2) |
| Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough. Brumlik M.J., Voordouw G.
J. Bacteriol. 171:4996-5004(1989) · UniProtKB (2) |
| Cloning and sequencing of the gene encoding cytochrome c553 from Desulfovibrio vulgaris Hildenborough. van Rooijen G.J.H., Bruschi M., Voordouw G.
J. Bacteriol. 171:3575-3578(1989) · UniProtKB (1) |
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