pH-Dependent Changes in ATP and ADP Affinity for the Tight Nucleotide-Binding Site of the Chloroplast Coupling Factor CF1 View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1990

AUTHORS

A. N. Malyan , O. I. Vitseva

ABSTRACT

The ATPase complex of chloroplasts (H+-ATPase, ATP-synthase) carries out synthesis (hydrolysis) of ATP coupled with transmembrane transport of hydrogen ions. This complex consists of a hydrophytic catalytic part called coupling factor CF1, and a hydrophobic part, CF0, the function of which is to translocate protons towards CF1. CF1 can bind as many as six nucleotide molecules /1/. After CF1 precipitation by ammonium sulfate with subsequent gel filtration, the enzyme retains about 1 mol of tightly bound nucleotides consisting mainly of ADP /2/. More... »

PAGES

1975-1978

Book

TITLE

Current Research in Photosynthesis

ISBN

978-94-010-6716-4
978-94-009-0511-5

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-009-0511-5_453

DOI

http://dx.doi.org/10.1007/978-94-009-0511-5_453

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1008300427


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