BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)=O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV)=O porphyrin at the peroxidatic heme . This state is spontaneously formed at am-bient conditions using either molecular O2 or H2O2. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology.

中文翻译：

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Y463M BthA 活性位点处的稳定铁卟啉

BthA 是一种二血红素酶，是细菌细胞色素 c 过氧化物酶超家族的成员，能够产生非常不寻常的 Fe(IV)Fe(IV)=O 氧化态，已知负责酶 MauG 中的长程氧化化学. 在这里，我们展示了安装规范的 Met 配体代替在与电子转移相关的 MauG 血红素处发现的 Tyr，导致在过氧化血红素处产生异常稳定的 Fe(IV)=O 卟啉的构建体。这种状态是在环境条件下使用分子 O2 或 H2O2 自发形成的。所得数据说明了如何在生物学中实现具有不可预见稳定性的弗莱尔铁。