[Study of the binding of substrates and paramagnetic Mn2+ ions with phosphoglycerate kinase by saturating ESR spectra of a spin-labelled protein].
A single SH-group of phosphoglycerate kinase from yeast was modified by mercury-containing spin label. The saturation curves of ESR spectra of the spin-labeled enzyme were studied. The paramagnetic ions of Mn2+ bound to the centre of ion nonspecific binding or active centre in the complex with ATP can influence the saturation of the spin-labeled enzyme. The saturation curves of the ESR signal of the spin-labeled enzyme in the presence of paramagnetic complex of CrATP were studied. It has been demonstrated that the second nonspecific centre of ATP binding is located at the active site of the enzyme (3-phosphoglycerate binding centre).
Vlasova
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II
Kuprin
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SP
D000255:Adenosine Triphosphate / Q000378:metabolism; D002413:Cations, Divalent; D004578:Electron Spin Resonance Spectroscopy; D008345:Manganese / Q000378:metabolism*; D010735:Phosphoglycerate Kinase / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013113:Spin Labels; D013379:Substrate Specificity
D002413:Cations, Divalent; D013113:Spin Labels; D008345:Manganese; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase
Izychenie sviazyvaniia substratov i paramagnitnykh ionov Mn2+ s fosfoglitseratkinazoĭ metodom nasyshcheniia spektrov EPR spin-mechenogo belka.