𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Energy-dependent changes in the ATP/ADP ratio at the tight nucleotide binding site of chloroplast ATP synthase

✍ Scribed by Alexander N. Malyan; Heinrich Strotmann

Publisher
Springer
Year
1994
Tongue
English
Weight
327 KB
Volume
42
Category
Article
ISSN
0166-8595

No coin nor oath required. For personal study only.

✦ Synopsis

Using DTT-modulated thylakoid membranes we studied fight nucleotide binding and ATP content in bound nucleotides and in the reaction mixture during [14C] ADP photophosphorylation. The increasing light intensity caused an increase in the rate of [14C] ADP incorporation and a decrease in the steady-state level of tightly bound nucleotides. Within the light intensity range from 11 to 710 w m -2, ATP content in bound nucleotides was larger than that in nucleotides of the reaction mixture; the most prominent difference was observed at low degrees of ADP phosphorylation. The increasing light intensity was accompanied by a significant increase of the relative ATP content in tightly bound nucleotides. The ratio between substrates and products formed at the tight nucleotide binding site during photophosphorylation was suggested to depend on the light-induced proton gradient across the thylakoid membrane.

πŸ“œ SIMILAR VOLUMES

Structure of the nucleotide-binding subu
Structure of the nucleotide-binding subunit B of the energy producer A1A0 ATP synthase in complex with adenosine diphosphate
✍ Kumar, Anil ;Manimekalai, Malathy Sony Subramanian ;GrΓΌber, Gerhard πŸ“‚ Article πŸ“… 2008 πŸ› International Union of Crystallography 🌐 English βš– 648 KB

A 1 A 0 ATP synthases are the major energy producers in archaea. Like the related prokaryotic and eukaryotic F 1 F 0 ATP synthases, they are responsible for most of the synthesis of adenosine triphosphate. The catalytic events of A 1 A 0 ATP synthases take place inside the A 3 B 3 hexamer of the A 1