Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation

scientific article published on 23 January 2013

Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2013PNAS..110.2117B
P356DOI10.1073/PNAS.1214741110
P932PMC publication ID3568300
P698PubMed publication ID23345443

P50authorBengt NordénQ4887827
P2093author name stringPer Lincoln
Tamás Beke-Somfai
P2860cites workThe structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolutionQ27627901
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysisQ27634146
Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolutionQ27644027
Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound NucleotidesQ27653878
Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncouplingQ27664519
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondriaQ27730864
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPaseQ27939194
Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP synthasesQ28611174
Direct observation of the rotation of F1-ATPaseQ29615360
A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisQ30438509
Determination of the partial reactions of rotational catalysis in F1-ATPaseQ30444018
Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthaseQ30497601
Torsional elasticity and energetics of F1-ATPaseQ30500093
Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPaseQ33942984
On the Mechanism of ATP Hydrolysis in F1-ATPaseQ34183062
The missing link between thermodynamics and structure in F1-ATPaseQ34327927
The molecular mechanism of ATP synthesis by F1F0-ATP synthaseQ34522937
Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthaseQ34721063
Domain motion of individual F1-ATPase β-subunits during unbiased molecular dynamics simulationsQ35064505
Catalytic sites of Escherichia coli F1-ATPaseQ35511384
Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPaseQ35651241
The role of the betaDELSEED-loop of ATP synthaseQ37160889
Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase.Q37490835
Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthaseQ42166624
Mechanical modulation of catalytic power on F1-ATPaseQ43033513
Structural fluctuation and concerted motions in F(1)-ATPase: A molecular dynamics studyQ43119164
Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthaseQ43147153
Mechanical control of ATP synthase function: activation energy difference between tight and loose binding sitesQ43225992
Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.Q50335878
Combining Quantum Mechanics Methods with Molecular Mechanics Methods in ONIOM.Q51630551
Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPasesQ68411204
Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPaseQ69933164
A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPaseQ74471754
Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotationsQ82619781
P433issue6
P407language of work or nameEnglishQ1860
P304page(s)2117-2122
P577publication date2013-01-23
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleRate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation
P478volume110

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cites work (P2860)
Q33919788Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases
Q38903183New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state.
Q30551514Phosphate release coupled to rotary motion of F1-ATPase
Q37648550Possible Involvement of F1F0-ATP synthase and Intracellular ATP in Keratinocyte Differentiation in normal skin and skin lesions
Q26780151Torque, chemistry and efficiency in molecular motors: a study of the rotary-chemical coupling in F1-ATPase
Q46903545What can be learned about the enzyme ATPase from single-molecule studies of its subunit F1?

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