Chromatium vinosum hydrogenase

Davidson, G., Choudhury, S. B., Gu, Z., Bose, K., Roseboom, W., Albracht, S. P. and Maroney, M. J. (2000) Structural examination of the nickel site in chromatium vinosum hydrogenase Redox state oscillations and structural changes accompanying reductive activation and CO binding. Biochemistry, 39, 7468-79. 

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.

NiFe]-hydrogenase and models State D, Chromatium vinosum 4.2 0.05-0.15 [314]... 

Bagley, K. A., Van Garderen, C. J., Chen, M., Duin, E. C., Albracht, S. P. and Woodruff, W. H. (1994) Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry, 33, 9229-36. 

Gessner, C., Stein, M., Albracht, S. P. and Lubitz, W. (1999) Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized ready state. /. Biol. Inorg. Chem., 4, 379-89. 

Happe, R. P., Roseboom, W. and Albracht, S. P. (1999) Pre-steady-state kinetics of the reactions of [NiFe]-hydrogenase from Chromatium vinosum with H2 and CO. Eur. J. Biochem., 259, 602-8. 

Van der Zwaan, J. W., Albracht, S. R, Fontijn, R. D. and Slater, E. C. (1985) Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen. FEES Lett., 179, 271-7. 

Bagley KA, Duin EC, RoseboomW, et al. 1995. Infrared-detectable groups sense changes in charge density on the nickel site in hydrogenase from Chromatium vinosum. Biochemistry 34 5527-35. 

Pershad HR, Duff JL, Heering HA, et al. 1999. Catalytic electron transport in Chromatium vinosum [NlFe]-hydrogenase application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H7H2 value. Biochemistry 38 8992-9. 

Surerus KK, Chen M, van der Zwaan JW, et al. 1994. Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mossbauer and mnltifreqnency EPR study. Biochemistry 33 4980-93. 

Van der Zwaan JW, Albracht SPJ, Fontijn RD, Roelofs YBM. 1986. EPR evidence for direct interaction of carbon monoxide with nickel in hydrogenase from Chromatium vinosum. Biochim Biophys Acta 872 208-15. 

A hydrogenase from chromatium vinosum has a similar structure.45313 There are still uncertainties about other nonprotein ligands such as HzO 452 453a... 

Albracht SPJ, van derZwaan JW, Fontijn RD, Slater EC (1986) On the possible redox states of nickel and the iron-sulphur cluster in hydrogenase from Chromatium vinosum. In Xavier AV (ed) Frontiers in bioinorganic Chemistry. VCH, Weinheim, pp 11-19... 

Reductive titrations of the [FeNij-hydrogenase from Chromatium vinosum were performed by variation of the H2-partial pressure [48]. Changes in the redox state of the active site were monitored by loss of the EPR signal. The reduction potential of the active site exhibits a pH dependence of -60 mV (pH unit)". This dependence suggests that the reduction of the active site is coupled with protonation. 

Aerobic bacteria such as Azotobacter vinelandii, Alcaligenes eutrophus, and Nocardia opaca, and facultative anaerobes, such as Escherichia coli and various species of Rhizobium and Bradyrhizobium (the symbionts of leguminous plants), also contain hydrogenase, as do photosynthetic bacteria such as Chromatium vinosum, Rhodobacter capsulatus (formerly Rhodopseudomonas capsulata), and Anabaena variabilis (a filamentous cyanobacterium). The thermophilic hydro-... 

Figure 25 Voltammetry of Alio chromatium vinosum NiFe hydrogenase adsorbed on aPGE electrode, under 0.1 atm Hj. Catalysis is diffusion controlled (note rotation-rate dependence) and rapid even at a potential where the [3Fe S] cluster will be reduced. (Adapted with permission from Biochemistry 1999, 38, 8992-8999. Copyright 1999 American Chemical Society.)...

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