巯基与血红蛋白的结构
Sulfhydryl groups and the structure of hemoglobin.
作者信息
RIGGS A F, WOLBACH R A
出版信息
J Gen Physiol. 1956 Mar 20;39(4):585-605. doi: 10.1085/jgp.39.4.585.
Abstract
- Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p(50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have little or no effect on the oxygen affinity. These effects are primarily associated with the binding of -SH groups, and are largely reversed on the addition of glutathione. -SH groups do not appear to be responsible for the Bohr effect. 2. Evidence is presented for the belief that the two hemes of each half-molecule of horse hemoglobin are situated on either side of a cluster of-SH groups. 3. The mechanism of interaction between the hemes is discussed. It is concluded that the reorganization of the protein architecture which accompanies oxygenation plays a central role in this interaction, in agreement with the views of Pauling and Wyman.
摘要
- 每摩尔血红蛋白添加2摩尔汞撒利、氯化汞、对氯汞苯甲酸（PCMB）或氢氧化甲基汞会极大地降低血红素 - 血红素相互作用（n），然而这些物质对氧亲和力（-log p(50)）有 quite different effects on the oxygen affinity (-log p(50)). 汞撒利和氯化汞在此浓度下均会增加氧亲和力，而PCMB和甲基汞对氧亲和力几乎没有影响。这些效应主要与 -SH基团的结合有关，并且在添加谷胱甘肽后很大程度上会逆转。-SH基团似乎与波尔效应无关。2. 有证据支持这样一种观点，即马血红蛋白每个半分子的两个血红素位于一组 -SH基团的两侧。3. 讨论了血红素之间的相互作用机制。得出的结论是，与氧合相伴的蛋白质结构重组在这种相互作用中起核心作用，这与鲍林和怀曼的观点一致。
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