The presence of redox-sensitive nickel in the periplasmic hydrogenase from Desulfovibrio gigas

A new and improved method for the purification of the periplasmic hydrogenase from Desulfovibrio gigas is described. This preparation of hydrogenase was found to contain 0.64 g atom of nickel per mole of protein. In the oxidized state, the hydrogenase exhibited an isotropic signal at g = 2.02 and a...

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Veröffentlicht in:	Biochemical and biophysical research communications 1982-05, Vol.106 (2), p.610-616
Hauptverfasser:	LeGall, J, Ljungdahl, P O, Moura, I, Peck, Jr, H D, Xavier, A V, Moura, J J, Teixera, M, Huynh, B H, DerVartanian, D V
Format:	Artikel
Sprache:	eng
Schlagworte:	Desulfovibrio - enzymology Desulfovibrio gigas Electron Spin Resonance Spectroscopy Hydrogenase Nickel - analysis Oxidation-Reduction Oxidoreductases - isolation & purification Oxidoreductases - metabolism purification
Online-Zugang:	Volltext
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