[Structural characteristics of paramagnetic analogs of enzyme-substrate complexes of phosphorylation coupling factors].
Mn2+-ion is linked to isolated chloroplast coupling factor CF-1 via the ATP bridge in the catalytically competent ternary complex as deduced from water proton relaxation rate measurements. Two essential SH-groups in CF-1 protein were modified with nitroxyl mercuric derivative as spin label. The substrate complex Ca2+-ATP is shown to induce the structural transition near the active site to the state with a stronger immobilized spin label. The distances between the paramagnetic metal ions and nitroxyl bound to the protein SH-group were evaluated as being in the range of 5-8,5 A for Cu2+ and 14-22 A for Mn2+.
D000255:Adenosine Triphosphate / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D008345:Manganese / Q000378:metabolism; D010085:Oxidative Phosphorylation; D010086:Oxidative Phosphorylation Coupling Factors / Q000032:analysis* / Q000378:metabolism; D010944:Plants / Q000378:metabolism*; D013113:Spin Labels; D013379:Substrate Specificity
D010086:Oxidative Phosphorylation Coupling Factors; D013113:Spin Labels; D008345:Manganese; D000255:Adenosine Triphosphate; D002118:Calcium
Strukturno-dinamicheskie kharakteristiki paramagnitnykh analogov ferment-substratnykh kompleksov sopriagaiushchego faktora fotofosforilirovaniia.