Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase (Q44901186)

7 December 2017

title

Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase (English)

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7 December 2017

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1

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7 December 2017

Alan E Senior

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7 December 2017

language of work or name

English

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publication date

18 May 2004

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Journal of Biological Chemistry

7 December 2017

published in

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7 December 2017

volume

279

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7 December 2017

issue

30

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7 December 2017

page(s)

31505-31513

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ATP synthesis driven by proton transport in F1F0-ATP synthase

7 December 2017

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The Escherichia coli FOF1 γM23K Uncoupling Mutant Has a Higher K0.5 for Pi. Transition State Analysis of This Mutant and Others Reveals That Synthesis and Hydrolysis Utilize the Same Kinetic Pathway

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F1-ATPase changes its conformations upon phosphate release

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The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgAT

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21 January 2018

Identifiers

DOI

10.1074/JBC.M404621200

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7 December 2017

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