Imperial College London

ProfessorThomasMeier

Faculty of Natural SciencesDepartment of Life Sciences

Visiting Professor
 
 
 
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Contact

 

t.meier Website

 
 
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Location

 

501Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Cheuk:2021:10.1042/BST20190936,
author = {Cheuk, A and Meier, T},
doi = {10.1042/BST20190936},
journal = {Biochemical Society Transactions},
pages = {541--550},
title = {Rotor subunits adaptations in ATP synthases from photosynthetic organisms},
url = {http://dx.doi.org/10.1042/BST20190936},
volume = {49},
year = {2021}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Driven by transmembrane electrochemical ion gradients, F-type ATP synthases are the primary source of the universal energy currency, adenosine triphosphate (ATP), throughout all domains of life. The ATP synthase found in the thylakoid membranes of photosynthetic organisms has some unique features not present in other bacterial or mitochondrial systems. Among these is a larger-than-average transmembrane rotor ring and a redox-regulated switch capable of inhibiting ATP hydrolysis activity in the dark by uniquely adapted rotor subunit modifications. Here, we review recent insights into the structure and mechanism of ATP synthases specifically involved in photosynthesis and explore the cellular physiological consequences of these adaptations at short and long time scales.
AU - Cheuk,A
AU - Meier,T
DO - 10.1042/BST20190936
EP - 550
PY - 2021///
SN - 0300-5127
SP - 541
TI - Rotor subunits adaptations in ATP synthases from photosynthetic organisms
T2 - Biochemical Society Transactions
UR - http://dx.doi.org/10.1042/BST20190936
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000647324100001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://portlandpress.com/biochemsoctrans/article/49/2/541/228451/Rotor-subunits-adaptations-in-ATP-synthases-from
UR - http://hdl.handle.net/10044/1/94602
VL - 49
ER -