Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.

Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.

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http://www.wikidata.org/entity/Q34055007

Q34055007

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The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinities Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis Characterization of the relationship between ADP- and epsilon-induced inhibition in cyanobacterial F1-ATPase Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis Alternative mitochondrial electron transfer for the treatment of neurodegenerative diseases and cancers: Methylene blue connects the dots.Kinetic and thermodynamic framework for P4-P6 RNA reveals tertiary motif modularity and modulation of the folding preferred pathway.Studies on the mechanism of oxidative phosphorylation: effects of specific F0 modifiers on ligand-induced conformation changes of F1.Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.The chloroplast ATP synthase features the characteristic redox regulation machinery.Kinetic properties of F0F1-ATPases. Theoretical predictions from alternating-site models Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.Nucleotide and Mg2+ dependency of the thermal denaturation of mitochondrial F1-ATPase.A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase.Structural mapping of the epsilon-subunit of mitochondrial H(+)-ATPase complex (F1).Thermodynamic analyses of nucleotide binding to an isolated monomeric β subunit and the α3β3γ subcomplex of F1-ATPase Interaction of ox heart mitochondrial F1-ATPase with immobilized ADP and ATP.Structural basis of proton translocation and force generation in mitochondrial ATP synthase.

P2860

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P2860

Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.

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http://www.wikidata.org/entity/Q34055007

description

1982 nî lūn-bûn

@nan

1982 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1982 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1982年の論文

@ja

1982年論文

@yue

1982年論文

@zh-hant

1982年論文

@zh-hk

1982年論文

@zh-mo

1982年論文

@zh-tw

1982年论文

@wuu