EPR evidence for nickel-substrate interaction in carbon monoxide dehydrogenase from Clostridium thermoaceticum

Journal Article · Thu Sep 30 04:00:00 EDT 1982 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(82)90880-4· OSTI ID:6329189

Ragsdale, S W; Ljungdahl, L G; DerVartanian, D V

Carbon monoxide dehydrogenase from Clostridium thermoaceticum contains two different Fe/sub 4/S/sub 4/ rhombic-type EPR resonances with g-values at 2.04, 1.94, 1.90 and 2.01, 1.86, 1.75, respectively. The enzyme after reacting wih CO or HCO/sub 3//sup -//CO/sub 2/ also reveals in EPR signal at g = 2.07 and 2.02. This signal, readily observed at 95K, is attributed to a Ni(III) interaction with a radical species formed from CO or HCO/sub 3//sup -//CO/sub 2/.

• Research Organization: Univ. of Georgia, Athens
• DOE Contract Number: AS09-79ER10499
• OSTI ID: 6329189
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 108:2; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
BIOCHEMICAL REACTION KINETICS
CARBON COMPOUNDS
CARBON MONOXIDE
CARBON OXIDES
CARBONIC ACID
CHALCOGENIDES
CLOSTRIDIUM
ELECTRON SPIN RESONANCE
ELEMENTS
ENZYMES
HYDROGEN COMPOUNDS
INORGANIC ACIDS
KINETICS
MAGNETIC RESONANCE
METALS
MICROORGANISMS
NICKEL
OXIDES
OXIDOREDUCTASES
OXYGEN COMPOUNDS
RADICALS
REACTION KINETICS
RESONANCE
STRUCTURAL CHEMICAL ANALYSIS
SUBSTRATES
TRANSITION ELEMENTS