Functional basis of electron transport within photosynthetic complex I
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Published version
Author(s)
Type
Journal Article
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 Issued
2021-09-10
Date Acceptance
2021-08-11
Citation
Nature Communications, 2021, 12 (5387), pp.1-8
ISSN
2041-1723
Publisher
Nature Research
Start Page
1
End Page
8
Journal / Book Title
Nature Communications
Volume
12
Issue
5387
Copyright Statement
© The Author(s) 2021. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
License URL
Sponsor
Engineering & Physical Science Research Council (EPSRC)
The Leverhulme Trust
Identifier
https://www.nature.com/articles/s41467-021-25527-1
Grant Number
EP/T031425/1
RPG-2018-183
Subjects
Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
NADH-UBIQUINONE OXIDOREDUCTASE
IRON-SULFUR CLUSTERS
PHOTOSYSTEM-I
EPR-SPECTRA
SUPEROXIDE-PRODUCTION
GENE ORGANIZATION
CHLOROPLAST NDH
4FE-4S CLUSTER
SUBUNIT
FLOW
Publication Status
Published
Date Publish Online
2021-09-10
