| Literature DB >> 2881810 |
Abstract
Sodium azide inhibited multi-site (steady-state) ATPase activity of E. coli F1 more than 90%, but did not affect uni-site (single-site) ATPase activity. Thus azide inhibited multi-site ATPase activity by lowering catalytic cooperativity. Consistent with this observation, azide changed the ligand-induced fluorescence response of aurovertin bound to F1.Entities:
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Year: 1987 PMID: 2881810 DOI: 10.1016/0014-5793(87)81526-0
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124