Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki. 1988

M Ogata, and S Kondo, and N Okawara, and T Yagi
Department of Chemistry, Shizuoka University.

Two ferredoxins, Fd I and Fd II, were isolated and purified from Desulfovibrio vulgaris Miyazaki. The major component, Fd I, is an iron-sulfur protein of Mr 12,000, composed of two identical subunits. The absorption spectra of Fd I and Fd II have a broad absorption shoulder near 400 nm characteristic of iron-sulfur proteins. The purity index, A400/A280, of Fd I is 0.69, and its millimolar absorption coefficient at 400 nm is 3.73 per Fe. It contains two redox centers with discrete redox behaviors. The amino acid composition and the N-terminal sequence of Fd I are similar to those of Fd III of Desulfovibrio africanus Benghazi and Fd II of Desulfovibrio desulfuricans Norway. Fd I does not serve as an electron carrier for the hydrogenase of D. vulgaris Miyazaki, but it serves as a carrier for pyruvate dehydrogenase of this bacterium. The evolution of H2 from pyruvate was observed by a reconstructed system containing purified hydrogenase, cytochrome C3, Fd I, partially purified pyruvate dehydrogenase, and CoA. The H2-sulfite reducing system can be reconstructed from the purified hydrogenase, cytochrome C3, Fd I and desulfoviridin (sulfite reductase), but the reaction rate is very slow compared to that of the crude extract at the same molar ratio of the components.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
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
D003901 Desulfovibrio A genus of gram-negative, anaerobic, rod-shaped bacteria capable of reducing sulfur compounds to hydrogen sulfide. Organisms are isolated from anaerobic mud of fresh and salt water, animal intestines, manure, and feces.
D005288 Ferredoxins Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

M Ogata, and S Kondo, and N Okawara, and T Yagi
December 1988, Biochimie,
M Ogata, and S Kondo, and N Okawara, and T Yagi
August 1988, Journal of biochemistry,
M Ogata, and S Kondo, and N Okawara, and T Yagi
March 1983, Journal of biochemistry,
M Ogata, and S Kondo, and N Okawara, and T Yagi
April 1985, Journal of biochemistry,
M Ogata, and S Kondo, and N Okawara, and T Yagi
August 1971, Biochimica et biophysica acta,
M Ogata, and S Kondo, and N Okawara, and T Yagi
June 1995, Biochemical and biophysical research communications,
M Ogata, and S Kondo, and N Okawara, and T Yagi
September 1991, Journal of biomolecular NMR,
M Ogata, and S Kondo, and N Okawara, and T Yagi
November 2008, Acta crystallographica. Section F, Structural biology and crystallization communications,
M Ogata, and S Kondo, and N Okawara, and T Yagi
February 1986, Journal of biochemistry,
M Ogata, and S Kondo, and N Okawara, and T Yagi
January 1996, Biochimie,
Copied contents to your clipboard!