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Structural biology: Toward the ATP synthase mechanism

scientific article published on November 2010

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20956969

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Structural biology: Toward the ATP synthase mechanism (English)

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8 November 2017

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Joachim Weber

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20956969

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8 November 2017

publication date

1 November 2010

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8 November 2017

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Nature Chemical Biology

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volume

6

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issue

11

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794-795

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https://scigraph.springernature.com/pub.10.1038/nchembio.458

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Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site

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https://pubmed.ncbi.nlm.nih.gov/20956969

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

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Phosphate release in F1-ATPase catalytic cycle follows ADP release.

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Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied

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Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis

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https://pubmed.ncbi.nlm.nih.gov/20956969

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DOI

10.1038/NCHEMBIO.458

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Europe PubMed Central

PubMed publication ID

20956969

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8 November 2017

PubMed publication ID

20956969

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PubMed publication ID

20956969

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8 November 2017

(Q42855081)

Structural biology: Toward the ATP synthase mechanism

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