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• W1994584174 abstract "57Fe-enriched samples of the soluble hydrogenase from Desulfovibrio desulfuricans (Norway) have been investigated in both the native (oxidized) and the dithionite-reduced states using Mössbauer spectroscopy. The data clearly show that the iron in this enzyme is predominantly in the form of iron-sulphur clusters which are closely similar to the [4Fe-4S] clusters found in a large number of ferredoxins, such as that from Bacillus stearothermophilus. There appear to be two [4Fe-4S] clusters. The iron-sulphur clusters in the oxidized protein are virtually diamagnetic, as indicated by Mössbauer, electron spin resonance and magnetic circular dichroic spectroscopy. On reduction by dithionite + methyl viologen, Mössbauer spectroscopy showed that only 50% of the [4Fe-4S] clusters were reduced. Even reduction with hydrogen up to a pressure of 23 GPa did not reduce the iron-sulphur clusters completely. An ESR signal due to a rapidly relaxing species with g = 2. 03, 1.89 was observed in the reduced protein, together with a weaker spectrum from a slower-relaxing spcies at g= 2.34, 2.12." @default.
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• W1994584174 date "1984-12-01" @default.
• W1994584174 modified "2023-10-14" @default.
• W1994584174 title "Spectroscopic studies of the nature of the iron clusters in the soluble hydrogenase from Desulfovibrio desulfuricans (strain Norway 4)" @default.
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• W1994584174 doi "https://doi.org/10.1111/j.1432-1033.1984.tb08605.x" @default.
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