Carbon monoxide dehydrogenase from Rhodospirillum rubrum
نویسندگان
چکیده
منابع مشابه
Carbon monoxide dehydrogenase from Rhodospirillum rubrum.
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 accept...
متن کاملLife on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resolution. The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site and a four-metal cubane. Surprisingly,...
متن کاملCarbon monoxide-dependent growth of Rhodospirillum rubrum.
Under dark, anaerobic conditions in the presence of sufficient nickel, Rhodospirillum rubrum grows with a doubling time of under 5 h by coupling the oxidation of CO to the reduction of H+ to H2. CO-dependent growth of R. rubrum UR294, bearing a kanamycin resistance cassette in cooC, depends on a medium nickel level ninefold higher than that required for optimal growth of coo+ strains.
متن کاملThe succinic dehydrogenase from Rhodospirillum rubrum.
Succinic dehydrogenase has usually been associated with a macromolecular intracellular unit (mitochondria) whenever the enzyme has been isolated. In an ultracentrifugal analysis of the composition of extracts of various organisms, Schachman et al. (1952) found that Rhodospirillum rubrum yielded particles with a wide range of sedimentation constants. Succinic dehydrogenase has been demonstrated ...
متن کاملHomoserine Dehydrogenase of Rhodospirillum rubrum
Homoserine dehydrogenase catalyzes the reductive conversion of aspartate P-semialdehyde to homoserine (l), which has been identified in several microorganisms as a precursor of three other amino acids. On the one hand, homoserine is converted to methionine, and through a separate sequence of reactions is transformed to threonine, a precursor of isoleucine (2). Recent studies (3-7) have provided...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1984
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.159.2.693-699.1984