The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743) : EPR and Mössbauer characterization

The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes th...

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Veröffentlicht in:European journal of biochemistry 1990-04, Vol.189 (2), p.381-386
Hauptverfasser: TEIXEIRA, M, MOURA, I, FAUQUE, G, DERVARTANIAN, D. V, LEGALL, J, PECK, H. D. JR, MOURA, J. J. G, HUYNH, B. H
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Sprache:eng
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Zusammenfassung:The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes the presence of a [3Fe-4S] center, either in the native (as isolated) or in the hydrogen-reduced states. In the native state, the non-heme iron atoms are arranged as two diamagnetic [4Fe-4S]2+ centers. Upon reduction, these two centers exhibit distinct and unusual Mössbauer spectroscopic parameters. The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR.
ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1990.tb15499.x