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Desulfovibrio desulfuricans hydrogenase

Hatchikian, E. C., Magro, V., Eorget, N. and Nicolet, Y. (1999) Carboxy-terminal processing of the large subunit of [Ee] hydrogenase from Desulfovibrio desulfuricans ATCC 7757. J. Bacterial., 181, 2947-52. [Pg.265]

Matias, P. M., Soares, C. M., Saraiva, L. M., Coelho, R., Morais, J., LeGall, J. and Carrondo, M. A. (2001) [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774 gene sequencing, three-dimensional structure determination and refinement at 1.8 angstrom and... [Pg.269]

Nicolet, Y., Piras, C., Legrand, P., Hatchikian, C. E. and Fontecilla-Camps, J. C. (1999) Desulfovibrio desulfuricans iron hydrogenase The structure shows unusual coordination to an active site Fe binuclear center. Structure Fold. Des., 7, 13-23. [Pg.271]

Fig. 8. BPR spectra of [3Fe-xS] clusters in oxidized hydrogenases, showing th influences of weak Ni-Fe-S electron-spin interactions, (a) Desulfovibrio desulfurican (strain Norway 4) hydrogenase, showing the spectrum of an isolated [3Fe-xS] cluster (b Chromatium vinosum hydrogenase the outer lines (Signal 2) correspond to interactio with Ni(lH) (c) Paracoccus denitrificans hydrogenase (d) Alcaligenes eutrophu membrane-bound hydrogenase. Spectra were recorded at approximately 20 K. Sample were provided by K. K. Rao, J. Serra, and K. Schneider. Fig. 8. BPR spectra of [3Fe-xS] clusters in oxidized hydrogenases, showing th influences of weak Ni-Fe-S electron-spin interactions, (a) Desulfovibrio desulfurican (strain Norway 4) hydrogenase, showing the spectrum of an isolated [3Fe-xS] cluster (b Chromatium vinosum hydrogenase the outer lines (Signal 2) correspond to interactio with Ni(lH) (c) Paracoccus denitrificans hydrogenase (d) Alcaligenes eutrophu membrane-bound hydrogenase. Spectra were recorded at approximately 20 K. Sample were provided by K. K. Rao, J. Serra, and K. Schneider.
Roseboom W, de Lacey AL, Fernandez VM, Hatchikian C, Albracht SPJ. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed via infrared spectroscopy. J Biol Inorg Chem. 2006 11(1) 102—18. [Pg.221]

Silakov A, Wenk B, Reijerse E, Albracht SPJ, Lubitz W. Spin distribution of the H-cluster in the Hox-CO state of the [FeFe] hydrogenase from Desulfovibrio desulfuricans HYSCORE and ENDOR study of 14N and 13C nuclear interactions. J Biol Inorg Chem. 2009 14(2) 301 13. [Pg.222]

Nicolet, Y., deLacey, A.L., Vemede, X., Fernandez, V.M., Hatchikian, E.C. and Fontecilla-Camps, J.C. 2001. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem.Soc. 123, 1596-1601. [Pg.265]

Steuber J, Cypionk H, Kroneck PMH (1994) Mechanism of dissimilatory sulfite reduction by Desulfovibrio desulfuricans purification of membrane-bound sulfite reductase and coupling with cytochrome c3 and hydrogenase. Arch Microbiol 162 255-260 Stille W, Triiper HG (1984) Adenylylsulfate reductase in some new sulfate reducing bacteria. Arch Microbiol 137 145-150... [Pg.145]


See other pages where Desulfovibrio desulfuricans hydrogenase is mentioned: [Pg.154]    [Pg.68]    [Pg.282]    [Pg.38]    [Pg.261]    [Pg.267]    [Pg.21]    [Pg.35]    [Pg.201]    [Pg.43]    [Pg.246]    [Pg.2303]    [Pg.2892]    [Pg.5561]    [Pg.6080]    [Pg.1579]    [Pg.1581]    [Pg.137]    [Pg.307]    [Pg.6079]    [Pg.281]    [Pg.421]    [Pg.314]    [Pg.239]    [Pg.218]    [Pg.82]   
See also in sourсe #XX -- [ Pg.504 , Pg.505 , Pg.506 , Pg.509 , Pg.510 ]




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Desulfovibrio

Desulfovibrio desulfuricans

Desulfovibrio hydrogenases

Hydrogenase

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