Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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2018 nî lūn-bûn

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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P1476

Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

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P2093

Hiroyuki Noji

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Makoto Genda

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Rikiya Watanabe

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Yasuyuki Kato-Yamada

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P2860

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

Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.

Energy transduction in the F1 motor of ATP synthase

Direct observation of the rotation of F1-ATPase

F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.

Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase

Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis.

P304

178-187

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P31

scholarly article

P356

10.1016/J.BPJ.2017.11.004

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P407

English

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P478

114

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P577

2018-01-01T00:00:00Z

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P698

29320685

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P932

5773760

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