Desulfovibrio vulgaris hydrogenase activation

Reductive Activation of Aerobically Purified Desulfovibrio vulgaris Hydrogenase Mossbauer Characterization of the Catalytic H Cluster... 

Hagen, W. R., van Berkel-Arts, A., Kruse-Wolters, K. M., Dunham, W. R. and Veeger, C. (1986) EPR of a novel high-spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough). FEBS Lett., 201, 158-62. 

Trofanchuk, O., Stein, M., Gessner, C., Lendzian, E, Higuchi, Y. and Lubitz, W. (2000) Single crystal EPR studies of the oxidized active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Inorg. Chem., 5, 364-4. 

Pierik AJ, Hagen WR, Redeker JS, et al. 1992. Redox properties of the iron-snlfnr clusters in activated iron-hydrogenase from Desulfovibrio vulgaris (Hildenbor-ough). Eur J Biochem 209 63-72. 

Marques MC, Coelho R, de Lacey AL, Pereira IAC, Matias PM. The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough a hydrogenase without a bridging ligand in the active site in its oxidised, as-isolated state. J Mol Biol. 2010 396(4) 893—907. 

Ogata H, Mizogushi Y, Mizuno N, et al. Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F suggestion for the initial activation site for dihydrogen. J Am Chem Soc. 2002 124(39) 11628-35. 

Foerster S, van Gastel M, Brecht M, Lubitz W. An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase. J Biol Inorg Chem. 2005 10(1) 51 62. 

The periplasmic [Fe]-hydrogenase from Desulfovibrio vulgaris (Hildenborough) exists in two different catalytic forms as isolated the protein is 02-insensitive upon reduction the protein becomes active and 02-sensitive [51], EPR-monitored redox titrations reveal a single reduction of the active site at a potential of -307 mV, just above the onset potential of H2 production. 

A second [FeNi]-hydrogenase structure, from Desulfovibrio vulgaris (Miyazaki F), revealed a similar active site cluster (PDB lh2a) [61]. Like the structure of the D. gigas enzyme, the active site cluster consists of a nickel ion coordinated by four cysteine residues, two of which form a bridge to the iron ion. The iron ion has three nonprotein ligands that are proposed to be the diatomics S=0, CO and CN mole-... 

Like pesticides, heavy metals are traditionally tested by enzyme inhibition or modulation of catalytic activity. Several metalloproteins behave as chelators for specific metals with no known catalytic reactions. Such heavy metal binding sites exist in metallothioneins and in various protein elements of bacterial heavy metal mechanisms and have been exploited for specific detection through affinity events. Nevertheless and as previously mentioned, bacterial resistance mechanisms can also be linked to catalytic pathways. For instance, c5rtochromes c3 and hydrogenases from sulfate and sulfur reducing bacteria [284,285] are well suited for bioremediation purposes because they can reduce various metals such as U(V) and Cr(VI) [286,287]. Cytochrome c3 has been reported to catalyse Cr(VI) and U(VI) reduction in Desulfovibrio vulgaris [288,289], suggesting... 

Lojou E, Durand MC, Dolla A, Bianco P (2002) Hydrogenase activity craitrol of Desulfovibrio vulgaris cell coated carbon electrodes biochemical and chemical factors influencing the mediated bioelectrocatalysis. Electroanalysis 14((13)) 913-922. doi 1040-0397/02/ 1307-0913... 

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