On the Mechanism of Regulation of Catalytic Activity of Chloroplast Coupling Factor 1 ATPase View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

A. N. Malyan , O. I. Vitseva

ABSTRACT

Chloroplast coupling factor one ATP ase (CF1 -ATPase) after its addition to the reaction mixture containing ADP and Mg2+ ions undergoes a slow reversible transition from a metastable active state to a stable steady state with low activity /1/. A similar transition occurs with the membrane-bound CF1 -ATPase /2/. The low level of the steady state CF1 -ATPase actrvity was shown to be due to the tight binding of ADP to a nucleotides binding site of the enzyme /1–4/. In this work we demonstrate that inactivation of CF1 -ATPase is accompanied by the gradual increase in the affinity of one nucleotide binding site to ADP and simultaneous decrease in the affinity of another site to ATP. The binding of ATP to the last site gives rise to the reactivation of CF1-ATPase. More... »

PAGES

21-24

Book

TITLE

Progress in Photosynthesis Research

ISBN

978-94-017-0518-9
978-94-017-0516-5

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-017-0516-5_5

DOI

http://dx.doi.org/10.1007/978-94-017-0516-5_5

DIMENSIONS

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