Studies on Spinach Ferredoxin-Nicotinamide Adenine Dinucleotide Phosphate Reductase

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Inhibitors of the transhydrogenase activity of spinach ferredoxin-Nicotinamide adenine dinucleotide phosphate reductase.

Boiled spinach extracts reversibly inhibit the transhydrogenase activity of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase. The inhibition is competitive with respect to NAD but noncompetitive with respect to NADPH. The inhibitor is most effective at a pH of about 8.0. The inhibitor is characterized as an organic acid but does not appear to be a carbohydrate or phosphoric acid...

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STIMULATION 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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On the reactivity of the sulfhydryl groups of ferredoxin nicotinamide adenine dinucleotide phosphate reductase.

The chloroplast flavoprotein has by amperometric titration four sulfhydryi groups and one disulfide per molecule. Inactivation by mercurials follows first order kinetics. From the order of this inactivation reaction with respect to mercurial, it is found that integrity of one sulfhydryl group is essential for catalytic activity. NADP affects the rate of inactivation of the flavoprotein by mercu...

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Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. I. Inhibition of ferredoxin nicotinamide adenine dinucleotide phosphate reductase by ferredoxin.

Purified ferredoxin has been shown to inhibit reactions mediated by the flavoprotein ferredoxin-NADP reductase. Ferredoxin inhibits the transfer of electrons from NADPH to ferricyanide (diaphorase activity) to NAD (transhydrogenase) and the photoreduction of pyridine nucleotides during the Hill reaction. On the basis of the kinetics of inhibition, it is suggested that the flavoprotein has two b...

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Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. II. Complex formation between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase and its relevance to pyridine nucleotide photoreduction.

It has been shown by difference spectroscopy that purified ferredoxin and ferredoxin-NADP reductase form a complex. The absorption maxima due to the interaction of the proteins are at 395, 469, and 495 nm. Bleached ferredoxin does not form such a complex. The stoichiometry of the complex is 2 molecules of ferredoxin per 1 molecule of flavoprotein. The complex is decomposed by salts but not by u...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1971

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)61780-6