Binding and hydrolysis of TNP-ATP by Escherichia coli F1-ATPase. (Q54593553)

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title

Binding and hydrolysis of TNP-ATP by Escherichia coli F1-ATPase. (English)

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Weber J

1

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Senior AE

series ordinal

2

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language of work or name

English

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publication date

1 February 1996

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Journal of Biological Chemistry

published in

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volume

271

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issue

7

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page(s)

3474-3477

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

cites work

1 reference

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Functional sites in F1-ATPases: location and interactions

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

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Coupling between catalytic sites and the proton channel in F1F0-type ATPases

21 January 2018

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Characterization of the tryptophan fluorescence from sarcoplasmic reticulum adenosinetriphosphatase by frequency-domain fluorescence spectroscopy.

21 January 2018

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The proton-ATPase of bacteria and mitochondria

21 January 2018

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Location and properties of pyrophosphate-binding sites in Escherichia coli F1-ATPase.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.7.3474

Asymmetry of Escherichia coli F1-ATPase as a Function of the Interaction of α-β Subunit Pairs with the γ and ∊ Subunits

21 January 2018

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Preparation and properties of 2'(or 3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate, an analog of adenosine triphosphate.

21 January 2018

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Inorganic and organic phosphate measurements in the nanomolar range

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.7.3474

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1 June 2018

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1 June 2018