Nascimento O R, Costa Ribeiro S, Bemski G
Biophys J. 1977 Aug;19(2):95-101. doi: 10.1016/S0006-3495(77)85572-0.
Copper introduced into met-myoglobin crystals occupies various sites as indicated by electron paramagnetic resonance parameters. Cu2+ (A) is probably liganded to histidine A10, lysine A14, and asparagine GH4 (Banaszak et al., 1965) and shows superhyperfine interaction with a single (imidazole) nitrogen. Cu2+ (B) and Cu2+ (C) correspond to other anisotropic sites described in less detail. Cu2+ (A) exhibits a transition to an isotropic form with a transition temperature of 40.5 degrees C. This transition indicates a conformational change in myoglobin and could correspond to a motion of A helix away from the GH section. The transition temperature is 7 degrees C higher than the one previously reported (Atanasov, 1971) for myoglobin in solution.
通过电子顺磁共振参数表明，引入到高铁肌红蛋白晶体中的铜占据了不同的位点。Cu2+(A)可能与组氨酸A10、赖氨酸A14和天冬酰胺GH4配位（巴纳扎克等人，1965年），并与单个（咪唑）氮显示出超超精细相互作用。Cu2+(B)和Cu2+(C)对应于描述较少的其他各向异性位点。Cu2+(A)在40.5摄氏度的转变温度下呈现向各向同性形式的转变。这种转变表明肌红蛋白发生了构象变化，可能对应于A螺旋远离GH片段的运动。该转变温度比先前报道的溶液中肌红蛋白的转变温度（阿塔纳索夫，1971年）高7摄氏度。
