Functional basis of electron transport within photosynthetic complex I

Katherine H. Richardson, John J. Wright, Mantas Šimėnas, Jacqueline Thiemann, Ana M. Esteves, Gemma McGuire, William K. Myers, John J. L. Morton, Michael Hippler, Marc M. Nowaczyk, Guy T. Hanke () and Maxie M. Roessler ()
Additional contact information
Katherine H. Richardson: Queen Mary University of London
John J. Wright: Queen Mary University of London
Mantas Šimėnas: University College London
Jacqueline Thiemann: Ruhr University Bochum
Ana M. Esteves: Queen Mary University of London
Gemma McGuire: Queen Mary University of London
William K. Myers: University of Oxford
John J. L. Morton: University College London
Michael Hippler: University of Münster
Marc M. Nowaczyk: Ruhr University Bochum
Guy T. Hanke: Queen Mary University of London
Maxie M. Roessler: Molecular Sciences Research Hub

Nature Communications, 2021, vol. 12, issue 1, 1-8

Abstract: Abstract Photosynthesis and respiration rely upon a proton gradient to produce ATP. In photosynthesis, the Respiratory Complex I homologue, Photosynthetic Complex I (PS-CI) is proposed to couple ferredoxin oxidation and plastoquinone reduction to proton pumping across thylakoid membranes. However, little is known about the PS-CI molecular mechanism and attempts to understand its function have previously been frustrated by its large size and high lability. Here, we overcome these challenges by pushing the limits in sample size and spectroscopic sensitivity, to determine arguably the most important property of any electron transport enzyme – the reduction potentials of its cofactors, in this case the iron-sulphur clusters of PS-CI (N0, N1 and N2), and unambiguously assign them to the structure using double electron-electron resonance. We have thus determined the bioenergetics of the electron transfer relay and provide insight into the mechanism of PS-CI, laying the foundations for understanding of how this important bioenergetic complex functions.

Date: 2021
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DOI: 10.1038/s41467-021-25527-1

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