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[Spectrofluorometric topography of the ATPase center of Ca2+-Mg2+-dependent ATPase of sarcoplasmic reticulum by means of platinum and palladium compounds].

The fluorescence of tryptophan residues in Ca2+--Mg2+-ATPase was studied in the presence of K2PtCl4, K2PdCl4 and 5-sulpho-8-mercaptochinolinate platinum and palladium. It has been shown that both first two compounds quenched the fluorescence dye to bonding with SH-groups in ATPase active centre, but the last two compounds influence the fluorescence by bonding with tryptophan residues. The distance between the SH-groups and tryptophan in the active centre was determined by Foerster--Galanin equation and was equal to 14 +/- 3 A.