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Article

A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase.

Journal of molecular biology - 18 Apr 2003

Bhaskar B, Immoos Chad E, Shimizu Hideaki, Sulc Filip, Farmer Patrick J, Poulos Thomas L

Abstract excerpt

The crystal structure of a cytochrome c peroxidase mutant where the distal catalytic His52 is converted to Tyr reveals that the tyrosine side-chain forms a covalent bond with the indole ring nitrogen atom of Trp51. We hypothesize that this novel bond results from peroxide activation by the heme iron followed by oxidation of Trp51 and Tyr52. This hypothesis has been tested by incorporation of a redox-inactive...

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Identifiers

PMID: 12684005
DOI: 10.1016/s0022-2836(03)00179-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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