The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway.
about
The rotary mechanism of the ATP synthase.Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling.Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport siteBinding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase.Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation.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.A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisIntergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis.Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases.Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Understanding structure, function, and mutations in the mitochondrial ATP synthase.ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptidesMedicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.The new unified theory of ATP synthesis/hydrolysis and muscle contraction, its manifold fundamental consequences and mechanistic implications and its applications in health and disease.Charge displacements during ATP-hydrolysis and synthesis of the Na+-transporting FoF1-ATPase of Ilyobacter tartaricus.Does F1-ATPase have a catalytic site that preferentially binds MgADP?Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein.Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics.Specific structural requirements for the inhibitory effect of thapsigargin on the Ca2+ ATPase SERCA.Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase.Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding.Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.Torque-coupled thermodynamic model for F_{o}F_{1}-ATPase.Identification of an uncoupling mutation affecting the b subunit of F1F0 ATP synthase in Escherichia coli.
P2860
Q24642754-01E9513C-C8E6-48BB-8464-C6744568F8AEQ27664519-DBC53BD8-DFA0-44FC-A467-E55E54ADA7E3Q27939194-B2DFD909-A6DE-4D44-A3AC-DB0E2CB91432Q30305571-865C3609-4E44-4D19-80C6-D57C56C51F8AQ30418606-365D8E91-4BFC-4A98-9495-31D9AA8D2E1EQ30429196-45EC8F8F-C76A-4B0D-A084-E348987C133CQ30435062-8FE3AD69-E13A-42B3-B69E-5A31EC4F9A25Q30438509-E5F62BED-19B5-40EB-A263-D94D26394246Q30471726-314E64E9-5332-44AE-82CA-4E57AB67E637Q30472484-BC2E4C6A-E530-44EC-9121-D6B89D1BF439Q33919788-AF502805-5966-491F-99B0-0F0CB09CD4BEQ34252667-A97D3404-EB09-4DFC-94D9-BFFC73475BD6Q34631137-9BDC2130-D2F9-4FA6-ACF9-D2FA5FC324CAQ35557164-F33EF64D-C2A0-4AE5-A1A6-896F0AD00462Q36525469-AA794419-AAC8-42E3-9144-D3ADC42EC6A3Q36525492-A060462D-0F71-4E54-98A3-098BF176C569Q39991977-162368B4-CF17-445A-8864-AA2A7DB470E4Q40253229-F68A7FA0-ABAE-4CAB-8871-79C6189FF555Q42204902-E1C18637-C863-437B-A31C-DBF24D2F2D8EQ42451287-8E1ABE62-6B6E-4A7E-9211-224882038F9EQ43147153-603A3A6C-51D7-44E5-83A2-D7319DDE3F9DQ44645471-EAC809B9-565B-4025-8044-C39F674CCBB0Q44768427-F28D2BC8-1DE3-40FE-A3E2-E661BB5A3C96Q44901186-D3BAE01E-6F00-466D-9561-D6604C36E984Q45218409-5180D7C1-46C7-4D4C-BBC3-22881A098164Q46531306-C70C4356-A8B8-4730-8E76-16671BF2CD09Q46615057-04E32FC7-A435-48BD-BDFC-0D79D5D4581FQ47895815-79DCB85D-373B-4697-B8EC-F69171EEE48A
P2860
The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway.
description
1997 nî lūn-bûn
@nan
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@ast
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@en
type
label
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@ast
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@en
prefLabel
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@ast
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@en
P2093
P356
P1433
P1476
The Escherichia coli FOF1 gamm ...... lize the same kinetic pathway.
@en
P2093
Al-Shawi MK
Ketchum CJ
Nakamoto RK
P304
12961-12969
P356
10.1021/BI971478R
P407
P577
1997-10-01T00:00:00Z