Molecular heterogeneity of ferredoxin:NADP+ oxidoreductase from the cyanobacterium Anabaena cylindrica

Rowell, Peter ; Diez, Jesus ; Apte, Shree K. ; Stewart, William D P. (1981) Molecular heterogeneity of ferredoxin:NADP+ oxidoreductase from the cyanobacterium Anabaena cylindrica Biochimica et Biophysica Acta (BBA) - Enzymology, 657 (2). pp. 507-516. ISSN 0005-2744

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2744(81)90335-1

Abstract

The enzyme ferredoxin:NADP+ oxidoreductase (EC 1.18.1.2) from whole filaments of Anabaena cylindrica can be separated into four major fractions by chromatography on phosphocellulose; chromatography using ferredoxin-Sepharose 4B proved to be less satisfactory in separating the fractions. The purified fractions, designated 1, 2, 3 and 4, all showed diaphorase and ferredoxin-dependent cytochrome c reductase activity. The major fractions present were 2 and 3 which were each obtained in an electrophoretically homogeneous state (forms 2 and 3) and represented 30-37% and 30-42%, respectively, of the total enzyme activity. Each was a monomeric species with a molecular weight of approx. 33 000 as determined by gel filtration and sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. Evidence for the presence of a 70 000 molecular weight dimer was also obtained. Forms 2 and 3 had isoelectric points of 5.75 and 6.0, respectively, had similar kinetic properties and were flavoproteins. Extracts of isolated heterocysts showed no form 2 or 3 activity but contained a single form which closely resembled one of the species present in fraction 4; fraction 1 may have been a purification artifact because it was not detected in crude extracts of the cyanobacterium.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Ferredoxin:NADP Oxidoreductase; Heterogeneity; (A. Cylindrica)
ID Code:793
Deposited On:25 Sep 2010 10:12
Last Modified:10 May 2011 15:00

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