Carbon monoxide dehydrogenase from Rhodospirillum rubrum. 1984

D Bonam, and S A Murrell, and P W Ludden

The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis. In vitro, this enzyme catalyzed a two-electron oxidation of CO to form CO2 as the product. The reaction was dependent on the addition of an electron acceptor. The enzyme was oxygen labile, heat stable, and resistant to tryptic and chymotryptic digestion. Optimum in vitro activity occurred at pH 10.0. A sensitive, hemoglobin-based assay for measuring dissolved CO levels is presented. The in vitro Km for CO was determined to be 110 microM. CO, through an unknown mechanism, stimulated hydrogen evolution in whole cells, suggesting the presence of a reversible hydrogenase in R. rubrum which is CO insensitive in vivo.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D002248 Carbon Monoxide Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed) Monoxide, Carbon
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000445 Aldehyde Oxidoreductases Oxidoreductases that are specific for ALDEHYDES. Aldehyde Oxidoreductase,Oxidoreductase, Aldehyde,Oxidoreductases, Aldehyde
D012247 Rhodospirillum rubrum Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.

Related Publications

D Bonam, and S A Murrell, and P W Ludden
September 2002, Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,
D Bonam, and S A Murrell, and P W Ludden
February 2004, Biochemistry,
D Bonam, and S A Murrell, and P W Ludden
October 2001, Proceedings of the National Academy of Sciences of the United States of America,
D Bonam, and S A Murrell, and P W Ludden
April 1995, Journal of bacteriology,
D Bonam, and S A Murrell, and P W Ludden
August 1992, Journal of bacteriology,
D Bonam, and S A Murrell, and P W Ludden
March 1987, The Journal of biological chemistry,
D Bonam, and S A Murrell, and P W Ludden
October 1989, The Journal of biological chemistry,
Copied contents to your clipboard!