PMID:9599011
| Citation |
Kuo, PH, Ketchum, CJ and Nakamoto, RK (1998) Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli. FEBS Lett. 426:217-20 |
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| Abstract |
All 21 native cysteines in the Escherichia coli F(0)F1 ATP synthase were replaced by alanines. In isolated E. coli membranes, ATP-dependent proton pumping, turnover of ATP hydrolysis and steady-state transition state thermodynamic parameters of the cysteine-less enzyme were similar to wild-type. The cysteine-less enzyme was solubilized in n-octyl beta-D-glucopyranoside, purified by affinity chromatography, and reconstituted into pre-formed liposomes made from E. coli lipids. The properties of the reconstituted, purified enzyme were not significantly different from the membranous enzyme. These data demonstrate that cysteine-less F(0)F1 is biochemically stable and has functionality similar to wild-type. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport, Active; Cysteine/chemistry; Detergents; Escherichia coli/enzymology; Liposomes; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/metabolism; Recombinant Proteins; Solubility; Structure-Activity Relationship; Thermodynamics |
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