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Biochemistry|July 8, 1980
Structure of the cytochrome c oxidase complex: labeling by hydrophilic and hydrophobic protein modifying reagentsL Prochaska, R Bisson, R A CapaldiBiochemistry|September 2, 1980
Binding of arylazidocytochrome c derivatives to beef heart cytochrome c oxidase: cross-linking in the high- and low-affinity binding sitesR Bisson, B Jacobs, R A CapaldiThe Journal of Biological Chemistry|June 27, 1997
Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthaseI Ogilvie, R Aggeler, R A CapaldiBiochemistry|December 27, 1977
Polypeptides in the succinate-coenzyme Q reductase segment of the respiratory chainR A Capaldi, J Sweetland, A MerliThe Journal of Biological Chemistry|February 11, 1994
Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studiesC Tang, S Wilkens, R A CapaldiBiochemistry|January 6, 1981
Interaction of succinate--ubiquinone reductase (complex II) with (arylazido)phospholipidsJ Girdlestone, R Bisson, R A CapaldiBiochemical Society Transactions|November 1, 1995
Conformational changes in the gamma and epsilon subunits are integral to the functioning of the Escherichia coli H(+)-pumping ATPase (ECF1F0)R A Capaldi, R Aggeler, S WilkensThe Journal of Biological Chemistry|August 1, 1997
Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complexR Aggeler, I Ogilvie, R A CapaldiBiochimica Et Biophysica Acta|June 1, 1995
Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunitR Aggeler, F Weinreich, R A CapaldiFEBS Letters|May 23, 1998
Trapping of conformations of the Escherichia coli F1 ATPase by disulfide bond formation. A state of the enzyme with all three catalytic sites of equal and low affinity for nucleotidesR Aggeler, G Grüber, R A CapaldiPageof 14