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Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide.

ABSTRACT: 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 A 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.

SUBMITTER: Hays Putnam AM

PROVIDER: S-EPMC2775101 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

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Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide.

Hays Putnam Anna-Maria A AM Lee Young-Tae YT Goodin David B DB

Biochemistry 20090101 1

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 A 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, hydro ...[more]

PMID: 19072042

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