Carbon monoxide dehydrogenase from Rhodospirillum rubrum

Journal Article · Sun Jul 01 04:00:00 EDT 1984 · J. Bacteriol.; (United States)

OSTI ID:5975850

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

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-election oxidation of CO to form CO/sub 2/ 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 K/sub m/ for CO was determined to be ..mu..M. 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. 38 references, 7 figures, 2 tables.

• Research Organization: Univ. of Wisconsin, Madison
• OSTI ID: 5975850
• Journal Information: J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 159:2; ISSN JOBAA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
CARBON COMPOUNDS
CARBON DIOXIDE
CARBON MONOXIDE
CARBON OXIDES
CHALCOGENIDES
CHEMICAL REACTIONS
ENZYME ACTIVITY
ENZYMES
IN VITRO
MEASURING METHODS
MICROORGANISMS
OXIDATION
OXIDES
OXIDOREDUCTASES
OXYGEN COMPOUNDS
PH VALUE
PURIFICATION
RHODOSPIRILLUM