一氧化碳与铁卟啉的结合。
Carbon monoxide binding to iron porphyrins.
作者信息
Collman J P, Brauman J I, Doxsee K M
出版信息
Proc Natl Acad Sci U S A. 1979 Dec;76(12):6035-9. doi: 10.1073/pnas.76.12.6035.
Abstract
The carbon monoxide affinities of iron complexes of meso-tetra (alpha, alpha, alpha, alpha-o-pivalamidophenyl)porphyrin (the "picket fence" porphyrin) and of a "picket fence" porphyrin derivative with an appended axial base have been measured in solution and compared with the CO affinities of various hemoproteins. The model complexes bind CO with much greater affinity than normal hemoproteins; the role of the steric bulk of distal residues in lowering the CO affinities of the hemoproteins is discussed. The significance of this lowered CO affinity is described with regard to endogenous CO. A discussion of mutant hemoglobins lacking distal residues that sterically inhibit the binding of CO is presented. The use of pressure units versus concentration units in equilibrium expressions is analyzed.
摘要
已在溶液中测量了中位四（α，α，α，α-邻新戊酰胺基苯基）卟啉（“栅栏”卟啉）的铁配合物以及带有附加轴向碱的“栅栏”卟啉衍生物对一氧化碳的亲和力，并将其与各种血红蛋白对一氧化碳的亲和力进行了比较。这些模型配合物与一氧化碳结合的亲和力比正常血红蛋白大得多；讨论了远端残基的空间位阻在降低血红蛋白对一氧化碳亲和力方面的作用。针对内源性一氧化碳描述了这种降低的一氧化碳亲和力的意义。还介绍了对缺乏空间抑制一氧化碳结合的远端残基的突变血红蛋白的讨论。分析了平衡表达式中压力单位与浓度单位的使用情况。
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