Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

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Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

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2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

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Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

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Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

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P1476

Chemomechanical coupling of F1-ATPase under hydrolysis conditions.

@en

P2093

Hiroyuki Noji

http://www.w3.org/2001/XMLSchema#string

Rikiya Watanabe

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P2860

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

Direct observation of the rotation of F1-ATPase

Temperature-sensitive reaction intermediate of F1-ATPase.

Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.

Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.

Is myosin a "back door" enzyme?

Mechanically driven ATP synthesis by F1-ATPase.

Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation

Thermodynamic efficiency and mechanochemical coupling of F1-ATPase.

P304

73-78

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P31

scholarly article

P356

10.2142/BIOPHYSICS.8.73

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P478

http://www.w3.org/2001/XMLSchema#string

P577

2012-04-13T00:00:00Z

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P698

27493523

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P932

4629648

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