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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >Why isn't 'standard' heme good enough for c-type and d_1-type cytochromes?
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Why isn't 'standard' heme good enough for c-type and d_1-type cytochromes?

机译：为什么“标准”血红素对c型和d_1型细胞色素不够好？

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摘要

This perspective seeks to discuss why biology often modifies the fundamental iron-protoporphyrin IX moiety that is the very versatile cofactor of many heme proteins.A very common modification is the attachment of this cofactor via covalent bonds to two (or rarely one) sulfur atoms of cys-teine residue side chains.This modification results in c-type cytochromes,which have diverse structures and functions.The covalent bonds are made in different ways depending on the cell type.There is little understanding of the reasons for this complexity in assembly routes but proposals for the rationale behind the covalent modification are presented.In contrast to the widespread c-type cytochromes,the d_1 heme is restricted to a single enzyme,the cytochrome cd_1 nitrite reductase that catalyses the one-electron reduction of nitrite to nitric oxide.This is an extensively derivatised heme;a comparison is drawn with another type of respiratory nitrite reductase in which the active site is a c-type heme,but the product ammonia.
机译：该观点旨在讨论生物学为什么经常修饰基本的原铁卟啉IX部分，而该部分是许多血红素蛋白的通用辅助因子。一种非常常见的修饰是，该辅助因子通过共价键连接到两个（或很少一个）硫原子上cys-teine残基侧链。这种修饰导致c型细胞色素具有不同的结构和功能。共价键根据细胞类型以不同的方式形成。人们对组装途径中这种复杂性的原因了解甚少与普遍的c型细胞色素相反，d_1血红素仅限于一种酶，即细胞色素cd_1亚硝酸盐还原酶，可将亚硝酸盐单电子还原为一氧化氮。这是一种广泛衍生的血红素;将其与另一种呼吸亚硝酸盐还原酶进行了比较，其中活性部位是c型血红素，但产物为氨。

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