Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites-Reference-Cited by-同舟云学术

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Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites

Published:2009-12-21 Issue:3 Volume:49 Page:401-403
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Beke-Somfai Tamás¹²,Lincoln Per¹,Nordén Bengt¹

Affiliation:

1. Department of Chemical and Biological Engineering, Physical Chemistry, Chalmers University of Technology, SE-412 96 Göteborg, Sweden

2. Protein Modelling Group MTA-ELTE, Institute of Chemistry, Eötvös Loránd University, P.O. Box 32, H-1538 Budapest, Hungary

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi901965c

Reference29 articles.

1. Energy, Life, and ATP (Nobel Lecture)

2. ATP Synthesis by Rotary Catalysis (Nobel lecture)

3. The molecular mechanism of ATP synthesis by F1F0-ATP synthase

4. Catalytic site forms and controls in ATP synthase catalysis

5. Hypothesis the mecanism of ATP synthase conformational change by rotation of the b-subunit

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2. Effect of carbonic inhibitors on enzymatic activity of isolated thylakoid CF1 ATPase;Reports of the National Academy of Sciences of Ukraine;2016-01-11

3. ATP Hydrolysis in the RecA–DNA Filament Promotes Structural Changes at the Protein–DNA Interface;Biochemistry;2015-07-27

4. From Metabolic Constraints on Individuals to the Dynamics of Ecosystems;Aquatic Functional Biodiversity;2015

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