Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.

doi:10.1021/ic100899k

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Article

Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.

Inorganic chemistry - 6 Sept 2010

Bowman Sarah E J, Bren Kara L

Abstract excerpt

The electron-donating properties of the axial His ligand to heme iron in cytochromes c (cyts c) are found to be correlated with the midpoint reduction potential (E(m)) in variants of Hydrogenobacter thermophilus cytochrome c(552) (Ht cyt c(552)) in which mutations have been made in and near the Cys-X-X-Cys-His (CXXCH) heme-binding motif. To probe the strength of the His-Fe(III) interaction, we have measured (13)C...

Topics

Amino Acid Motifs
Bacteria
Binding Sites
Cytochromes c
Heme
Histidine
Hydrogen Bonding
Iron
Mutation
Nuclear Magnetic Resonance, Biomolecular
Protein Binding

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Identifiers

PMID: 20666367
DOI: 10.1021/ic100899k
PMCID: PMC2933145

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