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Stuart D, Sandström M, Youssef HM, et al. Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. Plant Cell. 2021;33(8):2834-2849doi: 10.1093/plcell/koab150.
Stuart, D., Sandström, M., Youssef, H. M., Zakhrabekova, S., Jensen, P. E., Bollivar, D., & Hansson, M. (2021). Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. The Plant cell, 33(8), 2834-2849. https://doi.org/10.1093/plcell/koab150
Stuart, David, et al. "Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis." The Plant cell vol. 33,8 (2021): 2834-2849. doi: https://doi.org/10.1093/plcell/koab150
Stuart D, Sandström M, Youssef HM, Zakhrabekova S, Jensen PE, Bollivar D, Hansson M. Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. Plant Cell. 2021 Aug 31;33(8):2834-2849. doi: 10.1093/plcell/koab150. PMID: 34051099; PMCID: PMC8408499.
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Plant Cell. 2021 Aug 31;33(8):2834-2849. doi: 10.1093/plcell/koab150.

Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis.

The Plant cell

David Stuart, Malin Sandström, Helmy M Youssef, Shakhira Zakhrabekova, Poul Erik Jensen, David Bollivar, Mats Hansson

Affiliations

  1. Department of Biology, Lund University, Lund 22362, Sweden.
  2. Faculty of Agriculture, Cairo University, Giza 12613, Egypt.
  3. Department of Food Science, University of Copenhagen, Frederiksberg DK-1958, Denmark.
  4. Department of Biology, Illinois Wesleyan University, Bloomington, IL 61702-2900, USA.

PMID: 34051099 PMCID: PMC8408499 DOI: 10.1093/plcell/koab150

Abstract

Ferredoxins are single-electron carrier proteins involved in various cellular reactions. In chloroplasts, the most abundant ferredoxin accepts electrons from photosystem I and shuttles electrons via ferredoxin NADP+ oxidoreductase to generate NADPH or directly to ferredoxin dependent enzymes. In addition, plants contain other isoforms of ferredoxins. Two of these, named FdC1 and FdC2 in Arabidopsis thaliana, have C-terminal extensions and functions that are poorly understood. Here we identified disruption of the orthologous FdC2 gene in barley (Hordeum vulgare L.) mutants at the Viridis-k locus; these mutants are deficient in the aerobic cyclase reaction of chlorophyll biosynthesis. The magnesium-protoporphyrin IX monomethyl ester cyclase is one of the least characterized enzymes of the chlorophyll biosynthetic pathway and its electron donor has long been sought. Agroinfiltrations showed that the viridis-k phenotype could be complemented in vivo by Viridis-k but not by canonical ferredoxin. VirK could drive the cyclase reaction in vitro and analysis of cyclase mutants showed that in vivo accumulation of VirK is dependent on cyclase enzyme levels. The chlorophyll deficient phenotype of viridis-k mutants suggests that VirK plays an essential role in chlorophyll biosynthesis that cannot be replaced by other ferredoxins, thus assigning a specific function to this isoform of C-type ferredoxins.

© The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists.

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