Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations
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چکیده
منابع مشابه
Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations.
Ferredoxin reductase (Fd-reductase) supplies electrons to mitochondrial steroid hydroxylase cytochrome P450 enzymes via a [2Fe-2S] ferredoxin. Chemical labeling studies with bovine Fd-reductase have implicated Lys-243 as important in binding to bovine ferredoxin (Hamamoto, I., Kazutaka, K., Tanaka, S., and Ichikawa, Y. (1988) Biochim. Biophys. Acta 953, 207-213). We have used site-directed muta...
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Steady state rates of NADP reduction decline upon commencement of nitrite reduction in reconstituted chloroplast preparations. Similarly, steady state rates of nitrite reduction are lower, but not zero, during concurrent NADP reduction. These results imply that competition for substrate occurs and suggest that nitrite reduction can successfully compete for reduced ferredoxin, even at high rates...
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The reduction of ferredoxin-thioredoxin reductase (FTR) by plant-type ferredoxin plays an important role in redox regulation in plants and cyanobacteria. Nuclear magnetic resonance (NMR) was used to map the binding sites on Synechocystis ferredoxin for FTR. A gallium-substituted structural analog of this [2Fe-2S] ferredoxin was obtained by reconstituting the apoprotein in a refolding buffer con...
متن کاملInteractions between spinach ferredoxin-nitrite reductase and its substrates. Evidence for the specificity of ferredoxin.
Reduced ferredoxin can serve as electron donor in the 6-electron reduction of nitrite to ammonia catalyzed by spinach nitrite reductase. We have examined interactions between nitrite reductase and its substrates, ferredoxin and nitrite, with emphasis upon protein-protein interactions between ferredoxin and nitrite reductase. Ferredoxin, of the proteins tested, is the most effective in retarding...
متن کاملSTIMULATION OF OXYGEN UPTAKE OF FERREDOXIN-NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE-FERREDOXIN COMPLEX BY CYTOCHROME c*
The rate of oxygen uptake of spinach ferredoxin-NADP reductase-ferredoxin complex is increased up to ZO-fold by the addition of cytochrome c. Initiation of epinephrine and sulfite oxidation indicated an involvement of the superoxide anion radical in the stimulated oxidase reaction. The final product of the reaction was shown to be Hz0 instead of HsOt, which is the product of the flavoprotein-ca...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85311-5