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- W2000477860 abstract "The proton-translocating transmembrane pyridine nucleotide transhydrogenase of Escherichia coli is composed of two types of subunits, alpha and beta. The beta subunit has several membrane-spanning segments in the N-terminal region followed by a cytosolic C-terminal domain bearing a binding site for NADP(H). The N-terminal region contains at least one residue involved in the process of transmembrane proton translocation. Using site-directed mutagenesis cysteine residues were introduced at selected sites into the N-terminal region of the beta subunit. The pattern of labelling of these residues with 3-(N-maleimidyl propionyl)biocytin and other sulfhydryl reagents has shown that a model in which the N-terminal region of the beta subunit spans the membrane in eight segments is more likely than a previously proposed six segment model (Holmberg et al. (1994) Biochemistry 33, 7691-7700). The preferred model accounts for the site of labelling of a glutamate residue (Glu124) in the N-terminal domain by N,N-dicyclohexylcarbodiimide." @default.
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- W2000477860 date "1995-09-01" @default.
- W2000477860 modified "2023-10-16" @default.
- W2000477860 title "Organization in the Membrane of the N-Terminal Proton-Translocating Domain of the β Subunit of the Pyridine Nucleotide Transhydrogenase of Escherichia coli" @default.
- W2000477860 doi "https://doi.org/10.1006/bbrc.1995.2279" @default.
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