Ferredoxin-sulfite Reductase from a Cyanobacterium, Spirulina platensis(Biological Chemistry)
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概要
- 論文の詳細を見る
Ferredoxin-sulfite reductase (Fd-SiR) [hydrogen-sulfide: ferredoxin oxidoreductase, EC 1.8.7.1] from a cyanobacterium, Spirulina platensis, has been purified to homogeneity by a novel procedure. Subunit analysis by sodium dodecyl sulfate gel electrophoresis yielded a single protein band with a molecular weight of 63,000. In the presence of 0.1M potassium sulfate, gel filtration produced a value of 120,000, indicating the presence of a dimer in this ionic environment. A plot of ferredoxin concentration versus enzymatic (Fd-SiR) activity yielded a sigmoidal curve, giving a Hill coefficient (n) of 2.2. Purified Fd-SiR, in the oxidized form, has absorption maxima at 279, 388, and 590 nm. Thus the enzyme has the properties of a siroheme-containing protein.
- 社団法人日本農芸化学会の論文
- 1988-02-23
著者
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TAMURA Goro
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University
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Tamura Goro
Department Of Agricultural Chemistry Faclty Of Horticulture Chiba University
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KOGUCHI Osamu
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University
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Koguchi O
Chiba Univ. Matsudo Jpn
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Koguchi Osamu
Department Of Agricultural Chemistry Faclty Of Horticulture Chiba University
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