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- W2050851346 abstract "The absorption spectrum of the hydrogenase from Chromatium, which contains four iron atoms and four atoms of acid-labile sulfide, in 80% dimethylsulfoxide or hexamethylphosphoramide suggests the presence of a single [4Fe-4S] cluster. The EPR spectra of the oxidized enzyme in air, argon or carbon monoxide are the same with signals centered at g = 2.01. The enzyme reduced by hydrogen is EPR silent. The EPR spectrum is consistent with a [4Fe-4S] cluster. Chromatium hydrogenase and the hydrogenase from Proteus vulgaris show relative stability towards denaturation by sodium dodecyl sulfate (SDS), urea, guanidine and organic solvents." @default.
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- W2050851346 date "1980-11-01" @default.
- W2050851346 modified "2023-10-18" @default.
- W2050851346 title "Characterization and stability of hydrogenase from Chromatium" @default.
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- W2050851346 doi "https://doi.org/10.1016/0005-2744(80)90257-0" @default.
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