PreprintCited by 19Photosynthetic Processes and MechanismsMetalloenzymes and iron-sulfur proteinsPlant biochemistry and biosynthesis

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Tethering ferredoxin-NADP + reductase to photosystem I promotes photosynthetic cyclic electron transfer

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Preprint — published as 10.1093/plcell/koaf042

Abstract

Fixing CO 2 via photosynthesis requires ATP and NADPH. Linear electron transfer (LET) supplies both metabolites, yet depending on environmental conditions, additional ATP is required which can be generated by cyclic electron transfer (CET). How the balance between LET and CET is set remains largely unknown. Ferredoxin(FD)-NADP + reductase (FNR) has been suggested to act as the switch, channelling photosynthetic electrons to LET when it is bound to photosystem I (PSI) or CET when bound to cytochrome b 6 f . The essential role of FNR in LET precludes the use of a direct gene knock-out to test this hypothesis. We circumvented this problem by using CRISPR-Cas9 gene editing in Chlamydomonas reinhardtii to create a chimeric form of FNR tethered to PSI via PSAF. Chimeric FNR mutants exhibited impaired photosynthetic growth relative to the wild type, and decreased LET and non-photochemical quenching (NPQ) under high CO 2 conditions. However, higher rates of CET and increased NPQ were found in the mutants under low CO 2 or low O 2 conditions where CET is normally up-regulated. Thus, rather than PSI-FNR interactions promoting LET, tethering FNR to PSI promotes CET at the expense of LET and CO 2 fixation.

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Metadata

Authors
Emrich-Mills, T. Z., Proctor, M. S., Degen, G. E., Jackson, P. J., Richardson, K. H., Hawkings, F. R., Buchert, F., Hitchcock, A., Hunter, C. N., Mackinder, L. C. M., Hippler, M., & Johnson, M. P.
Affiliations
  • University of Sheffield (GB)
  • Diamond Light Source (GB)
  • University of Münster (DE)
  • University of York (GB)
  • Okayama University (JP)
Corresponding author
Johnson, Matthew P.
Venue
The Plant Cell
Publisher
openRxiv
Published
2024-11-03
Volume
37
Issue
3
ISSN
1040-4651 (ISSN-L)
OpenAlex
W4408129006
Cited by
19
References
1
Citations by year
2026: 15 · 2025: 4
FWCI
5.63
Type
journal article
Language
en
Open access
Locations
  • The Plant Cell (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
Funders
  • Leverhulme Trust (RPG-2021-345, RPG-2019-045)
  • Deutsche Forschungsgemeinschaft (HI 739/13-3, DFG FOR 5573)
  • Biotechnology and Biological Sciences Research Council (BB/W015269/1, BB/V006630/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
Keywords
ferredoxin-NADP+ reductase, photosystem I, cyclic electron flow, NADPH production, non-photochemical quenching, proton gradient, CO2 fixation, Chlamydomonas reinhardtii, CRISPR/Cas9 genome editing
MeSH terms
Electron Transport, Ferredoxin-NADP Reductase, NADP, Photosynthesis, Chlamydomonas reinhardtii, Photosystem I Protein Complex, CRISPR-Cas Systems

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