ELECTRON-PARAMAGNETIC RESONANCE EVIDENCE OF METAL-ION BINDING-SITES IN MICROCOCCUS-LYSODEIKTICUS (M-LUTEUS) F1-ATPASE

作     者：MOLLINEDO, F CANNISTRARO, S 

作者机构：UNIV PERUGIA DEPARTIMENTO FIS BIOF MOLECOL GRP I-06100 PERUGIA ITALY 

出 版 物：《BIOCHIMICA ET BIOPHYSICA ACTA》 (Biochim. Biophys. Acta Bioenerg.)

年 卷 期：1986年第848卷第2期

页      面：224-229页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

主　　题：F 1 -ATPase ESR Cu 2+ -binding site Mg 2+ -binding site ( M. lysodeikticus, M. luteus ) 

摘      要：Evidence is presented for the presence of divalent cation binding sites in purified F1-ATPase from Micrococcus lysodeikticus (Micrococcus luteus). Electron paramagnetic resonance studies of native F1-ATPase indicate that the enzyme binds Mn2+ and Cu2+. Scatchard-type plot for Mn2+ binding to the enzyme indicates the presence of 3-4 independent and identical sites with a dissociation constant of 18.3 .cntdot. 10-6 M. Cu2+ binds to the enzyme at only one kind of site(s). This Cu2+ binding site(s) is characterized by a moderately ionic ligand field provived by the protein and by a tetragonal symmetry of nitrogen and/or oxygen ligands. Competition studies indicate that Mg2+ binds at these Mn2+ and Cu2+ binding sites.