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

Tamás Beke-Somfai; Per Lincoln; Bengt Nordén

doi:10.1021/bi901965c

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

Tamás Beke-Somfai, Per Lincoln, Bengt Nordén

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Despite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. © 2009 American Chemical Society.

Original language	English (US)
Pages (from-to)	401-403
Number of pages	3
Journal	Biochemistry
Volume	49
Issue number	3
DOIs	https://doi.org/10.1021/bi901965c
State	Published - Jan 26 2010
Externally published	Yes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-11008-23
Acknowledgements: This Publication is based oil work Financed by King Abdullah University of Science and Technology (KAUST) (Grant KUK-11008-23).
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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

abstract = "Despite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. {\textcopyright} 2009 American Chemical Society.",

author = "Tam{\'a}s Beke-Somfai and Per Lincoln and Bengt Nord{\'e}n",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledged KAUST grant number(s): KUK-11008-23 Acknowledgements: This Publication is based oil work Financed by King Abdullah University of Science and Technology (KAUST) (Grant KUK-11008-23). This publication acknowledges KAUST support, but has no KAUST affiliated authors.",

year = "2010",

month = jan,

day = "26",

doi = "10.1021/bi901965c",

language = "English (US)",

volume = "49",

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journal = "Biochemistry",

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T1 - Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites

AU - Beke-Somfai, Tamás

AU - Lincoln, Per

AU - Nordén, Bengt

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledged KAUST grant number(s): KUK-11008-23 Acknowledgements: This Publication is based oil work Financed by King Abdullah University of Science and Technology (KAUST) (Grant KUK-11008-23). This publication acknowledges KAUST support, but has no KAUST affiliated authors.

PY - 2010/1/26

Y1 - 2010/1/26

N2 - Despite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. © 2009 American Chemical Society.

AB - Despite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. © 2009 American Chemical Society.

UR - http://hdl.handle.net/10754/598786

UR - https://pubs.acs.org/doi/10.1021/bi901965c

UR - http://www.scopus.com/inward/record.url?scp=74949093837&partnerID=8YFLogxK

U2 - 10.1021/bi901965c

DO - 10.1021/bi901965c

M3 - Article

C2 - 20000803

SN - 0006-2960

VL - 49

SP - 401

EP - 403

JO - Biochemistry

JF - Biochemistry

IS - 3

ER -

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

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