[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.
D000818:Animals; D001665:Binding Sites; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D007700:Kinetics; D010165:Palladium / Q000494:pharmacology*; D010984:Platinum / Q000494:pharmacology*; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry / Q000379:methods
D010984:Platinum; D010165:Palladium; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases
Spektrofluorimetricheskoe issledovanie topografii ATP-aznogo tsentra Ca2+-Mg2+-zavisimoĭ ATP-azy sarkoplazmaticheskogo retikuluma s pomoshch'iu soedineniĭ platiny i palladiia.