Article
The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling.
The Journal of biological chemistry - 19 Nov 2004
Motz Christian, Hornung Tassilo, Kersten Michael, McLachlin Derek T, Dunn Stanley D, Wise John G, Vogel Pia D
Abstract excerpt
We have used site-specific spin-labeling of single cysteine mutations within a water-soluble mutant of subunit b of the ATP synthase and employed electron spin resonance (ESR) spectroscopy to obtain information about the binding interactions of the b dimer with F1-ATPase. Interaction of b2 with a delta-depleted F1 (F1-delta) was also studied. The cysteine mutations used for spin-labeling were distributed...
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