| Literature DB >> 16691479 |
Zulfiqar Ahmad1, Alan E Senior.
Abstract
Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be one important component of Pi binding.Entities:
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Year: 2005 PMID: 16691479 DOI: 10.1007/s10863-005-9486-8
Source DB: PubMed Journal: J Bioenerg Biomembr ISSN: 0145-479X Impact factor: 3.853