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Article

Essential glycine in the proton channel of Escherichia coli transhydrogenase.

The Journal of biological chemistry - 14 Nov 2003

Yamaguchi Mutsuo, Stout C David

Abstract excerpt

The nicotinamide nucleotide transhydrogenases of mitochondria and bacteria are proton pumps that couple hydride ion transfer between NAD(H) and NADP(H) bound, respectively, to extramembranous domains I and III, to proton translocation by the membrane-intercalated domain II. Previous experiments h...

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PMID: 12952962
DOI: 10.1074/jbc.M308236200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12952962-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Essential glycine in the proton channel of Escherichia coli transhydrogenase.PMID 12952962Read ↗

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Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction.Semantic proximity Read ↗

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The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase.Semantic proximity Read ↗

Role of methionine-239, an amino acid residue in the mobile-loop region of the NADH-binding domain (domain I) of proton-translocating transhydrogenase.Semantic proximity Read ↗

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The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.Semantic proximity Read ↗

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