Kinetic modelling of the proton translocating CF0 CF1 -ATP synthase from spinach
| Autor: | Oliver Pänke, Bernd Rumberg |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
ATPase
Biophysics Photophosphorylation Chloroplast Binding Competitive Biochemistry Phosphates Adenosine Triphosphate Spinacia oleracea Structural Biology Genetics Enzyme kinetics Molecular Biology Binding Sites ATP synthase biology Chemiosmosis Chemistry Cell Biology Hydrogen-Ion Concentration Models Theoretical Carbamoyl phosphate synthetase Adenosine Diphosphate Kinetics Proton-Translocating ATPases Spectrometry Fluorescence Thylakoid biology.protein Mathematics ATP synthase alpha/beta subunits |
| Zdroj: | FEBS Letters. 383:196-200 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(96)00246-3 |
| Popis: | The rate of both ATP synthesis and hydrolysis catalysed by the thiol-modulated and activated ATP synthase from spinach is measured as a function of all substrates including the protons inside the thylakoid lumen. The most important findings are: (1) sigmoid kinetics with respect to H in + , (2) hyperbolic kinetics with respect to ADP, ATP and phosphate, with K m for phosphate and ADP decreasing upon increasing H in + , (3) binding of ADP and phosphate in random order and competitive to ATP. Simulation of the complete set of experimental data is obtained by a kinetic model featuring Boyer's binding-change mechanism. |
| Databáze: | OpenAIRE |
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