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@article{Richardson:2021:10.1038/s41467-021-25527-1,
author = {Richardson, K and Wright, JJ and Simenas, M and Thiemann, J and Esteves, AM and McGuire, G and Myers, WK and Morton, JJL and Hippler, M and Nowaczyk, MM and Hanke, G and Roessler, M},
doi = {10.1038/s41467-021-25527-1},
journal = {Nature Communications},
pages = {1--8},
title = {Functional basis of electron transport within photosynthetic complex I},
url = {http://dx.doi.org/10.1038/s41467-021-25527-1},
volume = {12},
year = {2021}
}

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TY  - JOUR
AB  - 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.
AU  - Richardson,K
AU  - Wright,JJ
AU  - Simenas,M
AU  - Thiemann,J
AU  - Esteves,AM
AU  - McGuire,G
AU  - Myers,WK
AU  - Morton,JJL
AU  - Hippler,M
AU  - Nowaczyk,MM
AU  - Hanke,G
AU  - Roessler,M
DO  - 10.1038/s41467-021-25527-1
EP  - 8
PY  - 2021///
SN  - 2041-1723
SP  - 1
TI  - Functional basis of electron transport within photosynthetic complex I
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-021-25527-1
UR  - https://www.nature.com/articles/s41467-021-25527-1
UR  - http://hdl.handle.net/10044/1/91037
VL  - 12
ER  -

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