Spartalian K, Lang G, Yonetani T
Biochim Biophys Acta. 1976 Apr 23;428(2):281-90. doi: 10.1016/0304-4165(76)90036-2.
57Fe-enriched complexes of hemoglobin and myoglobin with CO and O2 were photodissociated at 4.2 degrees K, and the resulting spectra were compared with those of the deoxy forms. Differences in both quadrupole splitting and isomer shift were noted for each protein, the photoproducts having smaller isomer shift and larger quadrupole splitting than the deoxy forms. The photoproducts of HbCO and HbO2 had narrow absorption lines, indicating a well-defined iron environment. The corresponding myoglobin species had broader absorption lines, as did both deoxy forms. The weak absorption lines of photodissociated NO complexes appeared to be wide, possibly indicating magnetic interaction with the unpaired electron of the nearby NO.
血红蛋白和肌红蛋白与一氧化碳和氧气形成的富含57Fe的配合物在4.2K下进行光解离，所得光谱与脱氧形式的光谱进行比较。每种蛋白质的四极分裂和同质异能位移均存在差异，光产物的同质异能位移比脱氧形式小，四极分裂比脱氧形式大。血红蛋白一氧化碳和血红蛋白氧气的光产物具有窄吸收线，表明铁环境明确。相应的肌红蛋白种类具有较宽的吸收线，脱氧形式也是如此。光解离的一氧化氮配合物的弱吸收线似乎很宽，可能表明与附近一氧化氮的未配对电子存在磁相互作用。
