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Colvert KK, Davis DJ. Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase. Photosynth Res. 1988;17(3):231-45doi: 10.1007/BF00035450.
Colvert, K. K., & Davis, D. J. (1988). Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase. Photosynthesis research, 17(3), 231-45. https://doi.org/10.1007/BF00035450
Colvert, K K, and Davis, D J. "Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase." Photosynthesis research vol. 17,3 (1988): 231-45. doi: https://doi.org/10.1007/BF00035450
Colvert KK, Davis DJ. Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase. Photosynth Res. 1988 Sep;17(3):231-45. doi: 10.1007/BF00035450. PMID: 24429770.
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Photosynth Res. 1988 Sep;17(3):231-45. doi: 10.1007/BF00035450.

Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase.

Photosynthesis research

K K Colvert, D J Davis

Affiliations

  1. Department of Chemistry and Biochemistry, University of Arkansas, 72701, Fayetteville, AR, USA.

PMID: 24429770 DOI: 10.1007/BF00035450

Abstract

Ferredoxin and the flavoprotein, ferredoxin: NADP reductase, have been covalently linked by incubation in the presence of a water soluble carbodiimide. The cross-linking reaction yields an adduct having a 1:1 stoichiometry. The adduct has depressed levels of diaphorase and NADPH oxidase activity and is inactive in reduction of cytochrome c using NADPH as an electron donor. Thus, although similar to an adduct described by Zanetti and coworkers [J Biol Chem 259: 6153-6157 (1984)] in its stoichiometry, the adduct described herein has significantly different enzymatic properties. It is suggested that this may be a reflection of differences in the interaction between the two proteins resulting from differences in experimental conditions in which the two adducts were prepared.

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