2006
DOI: 10.1073/pnas.0606254103
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Identification of a histidine-tyrosine cross-link in the active site of the cbb 3 -type cytochrome c oxidase from Rhodobacter sphaeroides

Abstract: The heme-copper oxidases constitute a superfamily of terminal dioxygen-reducing enzymes located in the inner mitochondrial or in the bacterial cell membrane. The presence of a mechanistically important covalent bond between a histidine ligand of the copper ion (Cu B) in the active site and a generally conserved tyrosine residue nearby has been shown to exist in the canonical cytochrome c oxidases. However, according to sequence alignment studies, this critical tyrosine is missing from the subfamily of cbb3-typ… Show more

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Cited by 54 publications
(54 citation statements)
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“…Recent studies using time-resolved optical spectroscopy and electrometric measurements on the B-family (21,22) confirm that the mechanism of O 2 reduction to water is essentially the same as in the A-family, including the role of the cross-linked, His-Tyr cofactor, which is widely thought to donate the electron and the proton needed to break the O 2 bond (9). C-family enzymes also contain the redox-active histidinetyrosine cofactor, and they probably use the same chemical reaction mechanism (23,24). These facts indicate that all 3 families share a common chemistry for O 2 reduction and a universal mechanism for proton pumping.…”
Section: Discussionmentioning
confidence: 81%
“…Recent studies using time-resolved optical spectroscopy and electrometric measurements on the B-family (21,22) confirm that the mechanism of O 2 reduction to water is essentially the same as in the A-family, including the role of the cross-linked, His-Tyr cofactor, which is widely thought to donate the electron and the proton needed to break the O 2 bond (9). C-family enzymes also contain the redox-active histidinetyrosine cofactor, and they probably use the same chemical reaction mechanism (23,24). These facts indicate that all 3 families share a common chemistry for O 2 reduction and a universal mechanism for proton pumping.…”
Section: Discussionmentioning
confidence: 81%
“…The cbb 3 -type enzymes are found only in bacteria, and are both structurally and functionally the most distant from their mitochondrial counterparts. The mechanistic H + /e − stoichiometry of proton translocation in these cbb 3 -type cytochrome c oxidases has remained controversial. A stoichiometric efficiency of only one-half that of the mitochondrial aa 3 -type enzyme was recently proposed to be related to adaptation of the organism to microaerobic environments.…”
mentioning
confidence: 99%
“…Cytochrome cbb 3 belongs to the superfamily of respiratory hemecopper oxidases that couple the reduction of molecular oxygen to proton translocation across the bacterial or mitochondrial membrane. The cbb 3 -type enzymes are found only in bacteria, and are both structurally and functionally the most distant from their mitochondrial counterparts.…”
mentioning
confidence: 99%
“…which is cross-linked to one of the histidine ligands to Cu B (21) and is approximately 4 Å from the O 2 binding site (16).…”
mentioning
confidence: 99%