Mechanisms of active transport in the F0F1 ATP synthase

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J]. NATURE, 1994, 370 (6491) : 621 - 628

[2] MONOCLONAL-ANTIBODY MODIFICATION OF THE ATPASE ACTIVITY OF ESCHERICHIA-COLI F1 ATPASE [J]. BIOCHEMISTRY, 1990, 29 (45) : 10387 - 10393

[3] DISULFIDE BOND FORMATION BETWEEN THE COOH-TERMINAL DOMAIN OF THE BETA-SUBUNITS AND THE GAMMA-SUBUNITS AND EPSILON-SUBUNITS OF THE ESCHERICHIA-COLI F1-ATPASE - STRUCTURAL IMPLICATIONS AND FUNCTIONAL CONSEQUENCES [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (16) : 9185 - 9191

[4] INTRODUCTION OF REACTIVE CYSTEINE RESIDUES IN THE EPSILON-SUBUNIT OF ESCHERICHIA-COLI F1 ATPASE, MODIFICATION OF THESE SITES WITH TETRAFLUOROPHENYL AZIDE MALEIMIDES, AND EXAMINATION OF CHANGES IN THE BINDING OF THE EPSILON-SUBUNIT WHEN DIFFERENT NUCLEOTIDES ARE IN CATALYTIC SITES [J]. BIOCHEMISTRY, 1992, 31 (11) : 2956 - 2961

[5] ARRANGEMENT OF THE EPSILON-SUBUNIT IN THE ESCHERICHIA-COLI ATP SYNTHASE FROM THE REACTIVITY OF CYSTEINE RESIDUES INTRODUCED AT DIFFERENT POSITIONS IN THIS SUBUNIT [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1995, 1230 (1-2): : 62 - 68

[6] CATALYTIC SITES OF ESCHERICHIA-COLI F1-ATPASE - CHARACTERIZATION OF UNISITE CATALYSIS AT VARIED PH [J]. BIOCHEMISTRY, 1992, 31 (03) : 878 - 885

[7] ALSHAWI MK, 1990, J BIOL CHEM, V265, P4402

[8] ALSHAWI MK, 1988, J BIOL CHEM, V263, P19633

[9] AVITAL S, 1991, J BIOL CHEM, V266, P7067

[10] THE F-O COMPLEX OF THE ATP SYNTHASE OF ESCHERICHIA-COLI CONTAINS A PROTON PATHWAY WITH LARGE PROTON POLARIZABILITY CAUSED BY COLLECTIVE PROTON FLUCTUATION [J]. BIOPHYSICAL JOURNAL, 1995, 68 (01) : 104 - 110

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J]. NATURE, 1994, 370 (6491) : 621 - 628

[2] MONOCLONAL-ANTIBODY MODIFICATION OF THE ATPASE ACTIVITY OF ESCHERICHIA-COLI F1 ATPASE [J]. BIOCHEMISTRY, 1990, 29 (45) : 10387 - 10393

[3] DISULFIDE BOND FORMATION BETWEEN THE COOH-TERMINAL DOMAIN OF THE BETA-SUBUNITS AND THE GAMMA-SUBUNITS AND EPSILON-SUBUNITS OF THE ESCHERICHIA-COLI F1-ATPASE - STRUCTURAL IMPLICATIONS AND FUNCTIONAL CONSEQUENCES [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (16) : 9185 - 9191

[4] INTRODUCTION OF REACTIVE CYSTEINE RESIDUES IN THE EPSILON-SUBUNIT OF ESCHERICHIA-COLI F1 ATPASE, MODIFICATION OF THESE SITES WITH TETRAFLUOROPHENYL AZIDE MALEIMIDES, AND EXAMINATION OF CHANGES IN THE BINDING OF THE EPSILON-SUBUNIT WHEN DIFFERENT NUCLEOTIDES ARE IN CATALYTIC SITES [J]. BIOCHEMISTRY, 1992, 31 (11) : 2956 - 2961

[5] ARRANGEMENT OF THE EPSILON-SUBUNIT IN THE ESCHERICHIA-COLI ATP SYNTHASE FROM THE REACTIVITY OF CYSTEINE RESIDUES INTRODUCED AT DIFFERENT POSITIONS IN THIS SUBUNIT [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1995, 1230 (1-2): : 62 - 68

[6] CATALYTIC SITES OF ESCHERICHIA-COLI F1-ATPASE - CHARACTERIZATION OF UNISITE CATALYSIS AT VARIED PH [J]. BIOCHEMISTRY, 1992, 31 (03) : 878 - 885

[7] ALSHAWI MK, 1990, J BIOL CHEM, V265, P4402

[8] ALSHAWI MK, 1988, J BIOL CHEM, V263, P19633

[9] AVITAL S, 1991, J BIOL CHEM, V266, P7067

[10] THE F-O COMPLEX OF THE ATP SYNTHASE OF ESCHERICHIA-COLI CONTAINS A PROTON PATHWAY WITH LARGE PROTON POLARIZABILITY CAUSED BY COLLECTIVE PROTON FLUCTUATION [J]. BIOPHYSICAL JOURNAL, 1995, 68 (01) : 104 - 110