Affiliation:
1. Pflanzenphysiologisches Institut der Universität Göttingen, Abt. Biochemie der Pflanzen und Botanisches Institut der Universität zu Köln
Abstract
Particles from Anacystis nidulans were obtained which - similar to preparations from spinachwere deficient in ferredoxin or in both ferredoxin and ferredoxin-NADP-reductase. The photosynthetic NADPH2-formation in these particles could be restored by addition of both these factors. The ferredoxin-NADP-reductase isolated from Anacystis closely ressembled in its enzymatical behaviour that enzyme from spinach. As previously described antibodies prepared against the spinach ferredoxin-NADP-reductase always inhibited the activities of the enzyme in spinach chloroplasts, regardless of whether the enzyme is bound to particles or made soluble. Contrary to this, in Anacystis these antibodies only affected the activities of the solubilized, but not of the particle-bound enzyme. Hence the reductase must be at least as tightly bound in the photosynthetic structure of Anacystis as it is in chloroplasts. The antibodies did not affect the ferredoxin-catalysed cyclic photophosphorylation in spinach and in Anacystis; this indicates that at least in spinach the ferredoxin-NADP-reductase is not involved in cyclic photophosphorylation.
Cited by
13 articles.
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