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Article

Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin.

Journal of the American Chemical Society - 9 May 2012

Reeder Brandon J, Svistunenko Dimitri A, Cooper Chris E, Wilson Michael T

Abstract excerpt

Tyrosine residues can act as redox cofactors that provide an electron transfer ("hole-hopping") route that enhances the rate of ferryl heme iron reduction by externally added reductants, for example, ascorbate. Aplysia fasciata myoglobin, having no naturally occurring tyrosines but 15 phenylalanines that can be selectively mutated to tyrosine residues, provides an ideal protein with which to study such...

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Identifiers

PMID: 22515641
DOI: 10.1021/ja211745g

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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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