PROBING STRUCTURE-FUNCTION RELATIONS IN HEME-CONTAINING OXYGENASES AND PEROXIDASES
PROBING STRUCTURE-FUNCTION RELATIONS IN HEME-CONTAINING OXYGENASES AND PEROXIDASES
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DOI：
10.1126/science.3358128
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发表时间：
1988-04-22
期刊：
影响因子：
56.9
通讯作者：
DAWSON, JH
中科院分区：
文献类型：
--
作者：
DAWSON, JH
结构因素影响的功能特性的情况下，血红素酶：细胞色素P-450，氯过氧化物酶，辣根过氧化物酶，仲胺单加氧酶进行检查。轴向配体的身份、血红素环境的性质以及血红素铁和血红素边缘的空间可及性结合联合收割机在确定每种酶的反应性中起主要作用。合成卟啉模型的重要性，在了解蛋白质的金属中心的性质强调。本文所述的结论来自生物化学和无机化学之间的界面研究。
Structural factors that influence functional properties are examined in the case of four heme enzymes: cytochrome P-450, chloroperoxidase, horseradish peroxidase, and secondary amine mono-oxygenase. The identity of the axial ligand, the nature of the heme environment, and the steric accessibility of the heme iron and heme edge combine to play major roles in determining the reactivity of each enzyme. The importance of synthetic porphyrin models in understanding the properties of the protein-free metal center is emphasized. The conclusions described herein have been derived from studies at the interface between biological and inorganic chemistry.