Unusual FTIR and EPR properties of the H2‐activating site of the cytoplasmic NAD‐reducing hydrogenase from Ralstonia eutropha

Soluble NAD‐reducing [NiFe]‐hydrogenase (SH) from Ralstonia eutropha (formerly Alcaligenes eutrophus) has an infrared spectrum with one strong band at 1956 cm−1 and four weak bands at 2098, 2088, 2081 and 2071 cm−1 in the 2150–1850 cm−1 spectral region. Other [NiFe]‐hydrogenases only show one strong...

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Bibliographic Details
Published in:	FEBS letters 2000-01, Vol.466 (2-3), p.259-263
Main Authors:	Happe, Randolph P., Roseboom, Winfried, Egert, Gabriele, Friedrich, Cornelius G., Massanz, Christian, Friedrich, Bärbel, Albracht, Simon P.J.
Format:	Article
Language:	English
Subjects:	[NiFe]-hydrogenase Active site Alcaligenes - enzymology Binding Sites BV, benzyl viologen Carbon monoxide Cyanide Cytoplasm - enzymology Electron Spin Resonance Spectroscopy EPR, electron paramagnetic resonance EXAFS, extended X-ray absorption fine structure FTIR, Fourier-transform infrared spectroscopy Hydrogen - metabolism MV, methyl viologen Oxidation-Reduction Oxidoreductases - chemistry Oxidoreductases - metabolism Ralstonia eutropha SH, soluble (cytoplasmic) hydrogenase Spectroscopy, Fourier Transform Infrared XAS, X-ray absorption spectroscopy
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