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Flavodiiron proteins 1-to-4 function in versatile combinations in O-2 photoreduction in cyanobacteria
Univ Turku, Dept Biochem, Mol Plant Biol, Turku, Finland.ORCID iD: 0000-0002-1556-0321
Univ Turku, Dept Biochem, Mol Plant Biol, Turku, Finland.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Univ Turku, Dept Biochem, Mol Plant Biol, Turku, Finland.
Univ Turku, Dept Biochem, Mol Plant Biol, Turku, Finland;Vrije Univ Amsterdam, Dept Phys & Astron, Biophys Photosynth, Amsterdam, Netherlands.
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2019 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 8, article id e45766Article in journal (Refereed) Published
Abstract [en]

Flavodiiron proteins (FDPs) constitute a group of modular enzymes widespread in Bacteria, Archaea and Eukarya. Synechocystis sp. PCC 6803 has four FDPs (Flv1-4), which are essential for the photoprotection of photosynthesis. A direct comparison of light-induced O-2 reduction (Mehler-like reaction) under high (3% CO2, HC) and low (air level CO2, LC) inorganic carbon conditions demonstrated that the Flv1/Flv3 heterodimer is solely responsible for an efficient steady-state O-2 photoreduction under HC, with flv2 and flv4 expression strongly down-regulated. Conversely, under LC conditions, Flv1/Flv3 acts only as a transient electron sink, due to the competing withdrawal of electrons by the highly induced NDH-1 complex. Further, in vivo evidence is provided indicating that Flv2/Flv4 contributes to the Mehler-like reaction when naturally expressed under LC conditions, or, when artificially overexpressed under HC. The O-2 photoreduction driven by Flv2/Flv4 occurs down-stream of PSI in a coordinated manner with Flv1/Flv3 and supports slow and steady-state O-2 photoreduction.

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ELIFE SCIENCES PUBLICATIONS LTD , 2019. Vol. 8, article id e45766
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-391945DOI: 10.7554/eLife.45766ISI: 000477603500001PubMedID: 31294693OAI: oai:DiVA.org:uu-391945DiVA, id: diva2:1346838
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Academy of Finland, 315119Academy of Finland, 82845Academy of Finland, 307335Available from: 2019-08-29 Created: 2019-08-29 Last updated: 2019-08-29Bibliographically approved

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