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  • Title: Characterization and stability of hydrogenase from Chromatium.
    Author: Strekas T, Antanaitis BC, Krasna AI.
    Journal: Biochim Biophys Acta; 1980 Nov 06; 616(1):1-9. PubMed ID: 6254569.
    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.
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