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J. Biol. Chem., Vol. 262, Issue 21, 9945-9947, 07, 1987

An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I

KA Macor, RS Czernuszewicz, MW Adams and TG Spiro

Resonance Raman spectra are reported for hydrogenase I and II from Clostridium pasteurianum. These spectra show overlapping bands with contributions from [4Fe-4S] clusters, known to be present in these enzymes, and from novel FeS centers of hitherto undefined structure. For hydrogenase I there are strong bands at 288 and 394 cm-1, which are seen in [2Fe-2S] proteins and in no other FeS species so far examined. In contrast these bands do not appear for hydrogenase II, whose resonance Raman spectrum is dominated by [4Fe-4S] cluster modes. These results provide the first structural information on the hydrogenase I FeS center involved in H2 activation and demonstrate structural differences between hydrogenase I and hydrogenase II.
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