Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
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Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP SynthaseHigh-resolution structure of the rotor ring of a proton-dependent ATP synthaseSubnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthaseThe INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthaseA genetic screen targeted on the FO component of mitochondrial ATP synthase in Saccharomyces cerevisiaeThe E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.Stepwise assembly of dimeric F(1)F(o)-ATP synthase in mitochondria involves the small F(o)-subunits k and i.Molecular mechanisms for generating transmembrane proton gradientsVoltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) familyThe adaptive evolution of the mammalian mitochondrial genomeArginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase.Inhibition of F1-ATPase rotational catalysis by the carboxyl-terminal domain of the ϵ subunit.Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase.Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.Realistic simulations of the coupling between the protomotive force and the mechanical rotation of the F0-ATPase.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.Consequences of the pathogenic T9176C mutation of human mitochondrial DNA on yeast mitochondrial ATP synthase.The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Understanding structure, function, and mutations in the mitochondrial ATP synthase.ExbD mutants define initial stages in TonB energizationCell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membraneThe where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase.The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli.Recombinant production and purification of the subunit c of chloroplast ATP synthase.Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transitionStochastic rotational catalysis of proton pumping F-ATPaseNeuronal pigmented autophagic vacuoles: lipofuscin, neuromelanin, and ceroid as macroautophagic responses during aging and disease.Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits.Assembly of F0 in Saccharomyces cerevisiae.Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hHV1.Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.Co-evolution of primordial membranes and membrane proteinsIdentification of G8969>A in mitochondrial ATP6 gene that severely compromises ATP synthase function in a patient with IgA nephropathy.Recent advances in structure-functional studies of mitochondrial factor B.Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.Molecular Regulation of the Mitochondrial F(1)F(o)-ATPsynthase: Physiological and Pathological Significance of the Inhibitory Factor 1 (IF(1)).
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P2860
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@ast
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@en
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@nl
type
label
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@ast
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@en
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@nl
prefLabel
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@ast
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@en
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@nl
P2093
P2860
P1433
P1476
Mechanics of coupling proton movements to c-ring rotation in ATP synthase.
@en
P2093
Christine M Angevine
Oleg Y Dmitriev
Robert H Fillingame
P2860
P356
10.1016/S0014-5793(03)01101-3
P407
P577
2003-11-01T00:00:00Z