来自人血红蛋白的两种不可逆半色素的铁位点结构，未处理以及在β链的MetD6(55)处氧化为亚砜。
Iron site structure of two irreversible hemichromes from human hemoglobin, untreated and oxidized to sulfoxide at MetD6(55)beta.
作者信息
Della Longa S, Amiconi G, Artan Salah O, Ascone I, Barteri M, Bertollini A, Bianconi A, Congiu Castellano A
机构信息
Dipartimento di Medicina Sperimentale, Università dell'Aquila, Italy.
出版信息
Biochim Biophys Acta. 1996 May 2;1294(1):72-6. doi: 10.1016/0167-4838(95)00270-7.
The Fe K-edge X-ray absorption near-edge structure (XANES) spectra of two irreversible human hemichromes, spontaneously formed from HbA and HbMetSO (a hemoglobin derivative, where MetD6(55)beta has been previously oxidized to sulfoxide by chloramine T) were determined. The results show that the hemichrome from HbMetSO is characterized by the distal histidyl imidazole moved within the bonding distance of the heme iron. Such structure is different from that of the hemichrome spontaneously produced from native human hemoglobin, which probably has a hydroxide group as sixth heme ligand.
测定了由HbA和HbMetSO（一种血红蛋白衍生物，其中MetD6(55)β先前已被氯胺T氧化为亚砜）自发形成的两种不可逆人高铁血红素的铁K边X射线吸收近边结构（XANES）光谱。结果表明，HbMetSO形成的高铁血红素的特征是远端组氨酸咪唑移动到了血红素铁的键合距离内。这种结构与天然人血红蛋白自发产生的高铁血红素不同，后者可能有一个羟基作为第六个血红素配体。
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