X-ray absorption spectroscopy of nickel in the hydrogenase from Desulfovibrio gigas

Journal Article · Wed Oct 31 04:00:00 EST 1984 · J. Am. Chem. Soc.; (United States)

DOI:https://doi.org/10.1021/ja00334a078· OSTI ID:6104478

Scott, R A; Wallin, S A; Czechowski, M; DerVartanian, D V; LeGall, J; Peck, Jr, H D; Moura, I

Results of preliminary X-ray absorption spectroscopic studies of the Desulfovibrio gigas enzyme indicate that the nickel is reduced from Ni(III) to Ni(II) upon H/sub 2/ reduction of the oxidized enzyme and that the ligands are bound to the nickel through the S atoms. Hydrogenase from Desulfovibrio gigas exhibited a single bond on disc acrylamide gel electrophoresis, and hydrogenase activity was determined by H/sub 2/ evolution assay.

• Research Organization: Univ. of Illinois, Urbana
• OSTI ID: 6104478
• Journal Information: J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 106:22; ISSN JACSA
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400104* -- Spectral Procedures-- (-1987)
400201 -- Chemical & Physicochemical Properties
400301 -- Organic Chemistry-- Chemical & Physicochemical Properties-- (-1987)
ABSORPTION SPECTROSCOPY
CHEMICAL ANALYSIS
COMPLEXES
ELEMENTS
ENZYMES
HYDROGENASES
METALS
NICKEL
NICKEL COMPLEXES
OXIDOREDUCTASES
SPECTROSCOPY
TRANSITION ELEMENT COMPLEXES
TRANSITION ELEMENTS
X-RAY SPECTROSCOPY