By LG Ljungdahl, MW Adams, LL Barton, JG Ferry, MK Johnson (Eds.)
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Additional info for Biochemistry and Physiology of Anaerobic Bacteria
1999) showed a terminal water molecule to coordinate to Fe2. Each iron atom is terminally coordinated by one CO and one CN-. The coordination of Fe1 is completed by the additional bridging cysteinyl sulfur. For Fe2, the sixth coordination site may be empty, as in the D. desulfuricans enzyme (Nicolet et al. 1999), or occupied by a solvent molecule, as observed in the C. pasteurianum enzyme (Peters et al. 1999). The assignment for the diatomic ligands is supported by infrared spectroscopic evidence (Pierik et al.
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.
Vinosum hydrogenase (Happe et al. 1999). 8 mM hydrogen (equivalent to 1 bar; Nia-SR state), a transient Nia-C* state was detected within 10 ms when the solution was mixed with CO-saturated buffer (in the dark). Thereafter, a rapid decline of the Nia-C* state was noticed (conversion into Nia-S·CO). The sample obtained at 10 ms could be converted to the Nia-L* state by illumination at 30K. Raising the temperature to 200K did not reverse process; instead a state was detected in which CO was directly bound to nickel (Nia*·CO).