Biochemistry and Physiology of Anaerobic Bacteria by LG Ljungdahl, MW Adams, LL Barton, JG Ferry, MK Johnson

By LG Ljungdahl, MW Adams, LL Barton, JG Ferry, MK Johnson (Eds.)

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After the heterolytic splitting, the two reducing equivalents from the hydride are rapidly taken up by the Fe-Fe site (one electron) and the attached proximal cluster (one electron). Subsequently, the electron is transferred from the proximal cluster to the other Fe-S clusters in the enzyme. Under equilibrium conditions, the proximal cluster in the active enzyme appears to be always in the oxidized [4Fe-4S]2+ state (Popescu and Münck 1999). Protons are not shown. J. Albracht References Albracht SPJ.

The assumption of three CO groups, two end-on ones and one bridging one, in the C. pasteurianum enzyme crystals, prepared under nitrogen in the presence of 2 mM dithionite (Fig. 1B), can explain the bands at 2007, 1983, and 1847 cm-1, respectively, in the aerobic inactive D. vulgaris enzyme. The two CN bands (2106 and 2087 cm-1) found in the latter enzyme can explain one of the diatomic ligands on each iron atom in the former enzyme. In the C. pasteurianum enzyme crystals prepared with dithionite under nitrogen an oxygen species is bound to Fe2.

1988). In an effort to obtain more information on the electronic properties of this unusual H cluster and to gain further insights into the reductive activation process of D. vulgaris hydrogenase, we used Mössbauer spectroscopy to characterize in detail the Fe-S clusters in samples of D. vulgaris enzyme equilibrated at different redox potentials during a reductive titration. A total of five samples (as-purified, -110 mV, -310 mV, -350 mV, and CO reacted) were studied. Details of the study are published elsewhere (Pereira et al.

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