Abstract
Carbon monoxide dehydrogenase (Cdh) has been anaerobically purified from Methanosarcina frisia Gö1. The enzyme is a Ni2+-, Fe2+-, and S2--containing alpha2beta2 heterotetramer of 214 kDa with a pI of 5.2 and subunits of 94 and 19 kDa. It has a Vmax of 0.3 mmol of CO min-1 mg-1 and Km values for CO and methyl viologen of approximately 0.9 mM and 0.12 mM, respectively. EPR spectroscopy on the reduced enzyme showed two overlapping signals: one indicative for 2 (4Fe-4S)+ clusters and a second signal that is atypical for standard Fe/S clusters. The latter was, together with high-spin EPR signals of the oxidized enzyme tentatively assigned to an Fe/S cluster of high nuclearity.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Aldehyde Oxidoreductases / chemistry
-
Aldehyde Oxidoreductases / genetics*
-
Aldehyde Oxidoreductases / metabolism*
-
Amino Acid Sequence
-
Base Sequence
-
Carbon Monoxide / metabolism
-
Electron Spin Resonance Spectroscopy
-
Gene Expression Regulation, Bacterial
-
Gene Expression Regulation, Enzymologic*
-
Genes, Bacterial*
-
Iron-Sulfur Proteins / biosynthesis
-
Iron-Sulfur Proteins / chemistry
-
Iron-Sulfur Proteins / genetics
-
Kinetics
-
Methanosarcina / enzymology*
-
Methanosarcina / genetics*
-
Molecular Sequence Data
-
Multienzyme Complexes / chemistry
-
Multienzyme Complexes / genetics*
-
Multienzyme Complexes / metabolism*
-
Multigene Family*
-
Operon*
-
Paraquat
-
Restriction Mapping
-
Sequence Homology, Amino Acid
Substances
-
Iron-Sulfur Proteins
-
Multienzyme Complexes
-
Carbon Monoxide
-
Aldehyde Oxidoreductases
-
carbon monoxide dehydrogenase
-
Paraquat
Associated data
-
GENBANK/L26486
-
GENBANK/L26487