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Article

Heme attachment motif mobility tunes cytochrome c redox potential.

Biochemistry - 23 Oct 2007

Michel Lea V, Ye Tao, Bowman Sarah E J, Levin Benjamin D, Hahn Megan A, Russell Brandy S, Elliott Sean J, Bren Kara L

Abstract excerpt

Hydrogen exchange (HX) rates and midpoint potentials (Em) of variants of cytochrome c from Pseudomonas aeruginosa (Pa cyt c551) and Hydrogenobacter thermophilus (Ht cyt c552) have been characterized in an effort to develop an understanding of the impact of properties of the Cys-X-X-Cys-His pentapeptide c-heme attachment (CXXCH) motif on heme redox potential. Despite structural conservation of the CXXCH motif, Ht...

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Identifiers

PMID: 17900177
DOI: 10.1021/bi701177j
PMCID: PMC2606054

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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