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Article

Conserved glycine 232 in the ligand channel of ba3 cytochrome oxidase from Thermus thermophilus.

Biochemistry - 15 Jul 2014

McDonald William, Funatogawa Chie, Li Yang, Chen Ying, Szundi Istvan, Fee James A, Stout C David, Einarsdóttir Olöf

Abstract excerpt

Knowing how the protein environment modulates ligand pathways and redox centers in the respiratory heme-copper oxidases is fundamental for understanding the relationship between the structure and function of these enzymes. In this study, we investigated the reactions of O2 and NO with the fully reduced G232V mutant of ba3 cytochrome c oxidase from Thermus thermophilus (Tt ba3) in which a conserved glycine residue...

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Identifiers

PMID: 24937405
DOI: 10.1021/bi500289h
PMCID: PMC4216187

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