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Replacement of an Electron Transfer Pathway in Cytochrome c Peroxidase with a Surrogate Peptide,

机译:用替代肽替代细胞色素c过氧化物酶中的电子转移途径,

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摘要

A proposed electron transfer pathway in cytochrome c peroxidase was previously excised from the structure by design. The engineered channel mutant was shown to bind peptide surrogates without restoration of cyt c oxidation. Here, we report the 1.6 Å crystal structure of (N-benzimidazole-propionic acid)-Gly-Ala-Ala bound within the engineered channel. The peptide retains many features of the native electron transfer pathway: placement of benzimidazole at the position of the Trp-191 radical, hydrogen bonding to Asp235, and positioning of the C-terminus near the point where wild type CcP makes closest contact to cyt c. The inability of this surrogate pathway to restore function supports proposals that electron transfer requires the Trp-191 radical.
机译:先前通过设计从结构中切除了细胞色素c过氧化物酶中拟议的电子转移途径。该工程通道突变体显示出结合肽替代物而不恢复cyt c氧化。在这里,我们报告了工程通道内结合的(N-苯并咪唑-丙酸)-Gly-Ala-Ala的1.6Å晶体结构。该肽保留了天然电子转移途径的许多特征:将苯并咪唑置于Trp-191自由基的位置,氢键与Asp235的位置以及C端的位置靠近野生型CcP与cyt c最紧密接触的位置。该替代途径无法恢复功能,支持了电子转移需要Trp-191自由基的提议。

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