By LG Ljungdahl, MW Adams, LL Barton, JG Ferry, MK Johnson (Eds.)
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Extra resources for Biochemistry and Physiology of Anaerobic Bacteria
The RH has some very special properties, however: (1) it can exist in only two redox states (Nia-S and Nia-C*, Fig. J. 5. The reactions of hydrogen with the bimetallic sites in hydrogenases. A, Enzymes with a standard Ni-Fe active site. The binding of hydrogen to the Nia-S state leads to the Nia-C* state. It is assumed that the nickel ion is thereby oxidized and that the electron moves to the Fe-S clusters. For unknown reasons, in RH no further reaction with hydrogen is possible. In standard [NiFe]-hydrogenases only the Nia-C* and Nia-SR states are in rapid equilibrium with hydrogen (Coremans et al.
1990) near to the nickel atom, presumably spaced between the nickel and iron atoms (Volbeda et al. 1995, 1996) (Fig. 1A). For the D. vulgaris Miyazaki enzyme, this species has been proposed to be sulfur rather than oxygen (Higuchi et al. 1997). The O/S species blocks the rapid activation of hydrogen. Upon reductive activation, this species leaves the active site, presumably as H2O (or H2S). In this report, only the three active states are considered (Nia-S, Nia-C*, and Nia-SR) (Fig. 2). The states are observed in many [NiFe]-hydrogenases, like the ones from D.
Albracht References Albracht SPJ. 1994. Nickel hydrogenases: in search of the active site. Biochim Biophys Acta 1188:167–204. Albracht SPJ, Hedderich R. 2000. Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH: ubiquinone oxidoreductase (complex I) FEBS Lett 485:1–6. Bagley KA, Duin EC, Roseboom W, et al. 1995. Infrared-detectable groups sense changes in charge density on the nickel site in hydrogenase from Chromatium vinosum. Biochemistry 34:5527–35. Bagley KA, van Garderen CJ, Chen M, et al.
Biochemistry and Physiology of Anaerobic Bacteria by LG Ljungdahl, MW Adams, LL Barton, JG Ferry, MK Johnson (Eds.)