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Article

Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.

The journal of physical chemistry. B - 17 May 2012

Ly H Khoa, Utesch Tillmann, Díaz-Moreno Irene, García-Heredia José M, De La Rosa Miguel Ángel, Hildebrandt Peter

Abstract excerpt

Post-translational nitration of tyrosine is considered to be an important step in controlling the multiple functions of cytochrome c (Cyt-c). However, the underlying structural basis and mechanism are not yet understood. In this work, human Cyt-c variants in which all but one tyrosine has been substituted by phenylalanine have been studied by resonance Raman and electrochemical methods to probe the consequences...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 22540335
DOI: 10.1021/jp302301m

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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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