Heterologous plastoquinone production using a newly identified O₂‐dependent cyanobacterial hydroxylase
Abstract
Isoprenoid quinones constitute a class of redox lipids that are indispensable for electron transfer in a variety of cellular functions. For instance, plastoquinone, an integral component of plants, algae and Cyanobacteriota , plays a pivotal role in photosynthesis. Isoprenoid quinones are biosynthesised via evolutionary‐related pathways, in which some steps are still incompletely characterised. In this study, we confirm the identity of the PlqH enzyme, a flavin‐dependent monooxygenase (FMO) conserved in photosynthetic cyanobacteria, which possesses a regioselective hydroxylase activity required for plastoquinone biosynthesis. Phylogenetic analyses demonstrate that cyanobacterial PlqH homologues originated from FMOs involved in bacterial ubiquinone biosynthesis. The synthesis of plastoquinone by Escherichia coli was achieved by expressing two heterologous genes in a genetically engineered strain, which was optimised to produce plastoquinone levels comparable to those of natural ubiquinone. However, plastoquinone was unable to replace ubiquinone in several cellular processes in E. coli , suggesting that fine structural and thermodynamic constraints both play a significant role in the function of quinones.
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BibTeX
@article{rogermargueritat2026heterologous,
title = {{Heterologous plastoquinone production using a newly identified O₂‐dependent cyanobacterial hydroxylase}},
author = {Morgane Roger-Margueritat and Margot Beltran and Juliette Schnoebelen and Laura Flandrin and Wafa Rezali and Eline Michel and Sophie S. Abby and Fabien Pierrel},
journal = {FEBS Journal},
year = {2026},
month = nov,
doi = {10.1111/febs.70272},
url = {https://hal.science/hal-05302505v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Heterologous plastoquinone production using a newly identified O₂‐dependent cyanobacterial hydroxylase
AU - Morgane Roger-Margueritat
AU - Margot Beltran
AU - Juliette Schnoebelen
AU - Laura Flandrin
AU - Wafa Rezali
AU - Eline Michel
AU - Sophie S. Abby
AU - Fabien Pierrel
PY - 2026
DA - 2026/11/02
JO - FEBS Journal
DO - 10.1111/febs.70272
UR - https://hal.science/hal-05302505v1
AB - Isoprenoid quinones constitute a class of redox lipids that are indispensable for electron transfer in a variety of cellular functions. For instance, plastoquinone, an integral component of plants, algae and Cyanobacteriota , plays a pivotal role in photosynthesis. Isoprenoid quinones are biosynthesised via evolutionary‐related pathways, in which some steps are still incompletely characterised. In this study, we confirm the identity of the PlqH enzyme, a flavin‐dependent monooxygenase (FMO) conserved in photosynthetic cyanobacteria, which possesses a regioselective hydroxylase activity required for plastoquinone biosynthesis. Phylogenetic analyses demonstrate that cyanobacterial PlqH homologues originated from FMOs involved in bacterial ubiquinone biosynthesis. The synthesis of plastoquinone by Escherichia coli was achieved by expressing two heterologous genes in a genetically engineered strain, which was optimised to produce plastoquinone levels comparable to those of natural ubiquinone. However, plastoquinone was unable to replace ubiquinone in several cellular processes in E. coli , suggesting that fine structural and thermodynamic constraints both play a significant role in the function of quinones.
SN - 1742-464X
SN - 1742-4658
ER -