Studies on nitrate reductase of Clostridium perfringens. II. Purification and some properties of ferredoxin. 1979

S Seki, and M Hagiwara, and K Kudo, and M Ishimoto

A ferredoxin was purified from Clostridium perfringens by DEAE-cellulose chromatography and Sephadex G-50 gel filtration. It had absorption maxima at 390 and 280 nm. The molecular weight was estimated to be 6,000 by Sephadex gel filtration and from the results of amino acid analysis. The isoelectric point was 3.0. It contained four atoms of iron, four atoms of labile sulfur, and six cysteine residues. This ferredoxin as well as ferredoxin from C. pasteurianum acted as an electron donor for nitrate reductase from C. perfringens. The ferredoxin could also act as an electron donor for the hydrogenase from C. pasteurianum in hydrogen evolution.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009565 Nitrate Reductases Oxidoreductases that are specific for the reduction of NITRATES. Reductases, Nitrate
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D003016 Clostridium perfringens The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins. Clostridium welchii
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
D006859 Hydrogen The first chemical element in the periodic table with atomic symbol H, and atomic number 1. Protium (atomic weight 1) is by far the most common hydrogen isotope. Hydrogen also exists as the stable isotope DEUTERIUM (atomic weight 2) and the radioactive isotope TRITIUM (atomic weight 3). Hydrogen forms into a diatomic molecule at room temperature and appears as a highly flammable colorless and odorless gas. Protium,Hydrogen-1
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
D013455 Sulfur An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine. Sulfur-16,Sulfur 16

Related Publications

S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
December 1977, Journal of biochemistry,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
June 1973, Journal of biochemistry,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
October 1983, Journal of biochemistry,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
October 1973, The Japanese journal of experimental medicine,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
February 1971, Japanese journal of medical science & biology,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
October 1977, Biochimica et biophysica acta,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
January 1976, Annales de microbiologie,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
January 1977, Journal of biochemistry,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
February 1987, Journal of biochemistry,
S Seki, and M Hagiwara, and K Kudo, and M Ishimoto
July 1979, Journal of bacteriology,
Copied contents to your clipboard!