Burgess, Steven J., Hussein, Taha, Yeoman, Justin A., Iamshanova, Oksana, Chan, Kher Xing, Boehm, Marko, Behrends, Volker ORCID: https://orcid.org/0000-0003-4855-5497, Bundy, Jacob G., Bialek, Wojciech and Murray, James W. (2015) Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts. Plant Cell Physiology, 57 (1). ISSN 0032-0781

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Abstract

Under anoxic conditions the green alga Chlamydomonas
reinhardtii activates various fermentation pathways leading
to the creation of formate, acetate, ethanol and small
amounts of other metabolites including D-lactate and hydrogen.
Progress has been made in identifying the enzymes
involved in these pathways and their subcellular locations;
however, the identity of the enzyme involved in reducing
pyruvate to D-lactate has remained unclear. Based on sequence
comparisons, enzyme activity measurements, X-ray
crystallography, biochemical fractionation and analysis
of knock-down mutants, we conclude that pyruvate
reduction in the chloroplast is catalyzed by a tetrameric
NAD+-dependent D-lactate dehydrogenase encoded by
Cre07.g324550. Its expression during aerobic growth supports
a possible function as a ‘lactate valve’ for the export
of lactate to the mitochondrion for oxidation by cytochrome-
dependent D-lactate dehydrogenases and by glycolate
dehydrogenase. We also present a revised spatial model
of fermentation based on our immunochemical detection of
the likely pyruvate decarboxylase, PDC3, in the cytoplasm.

Item Type:	Article
Identifier:	10.1093/pcp/pcv167
Keywords:	Biohydrogen; Chlamydomonas; Fermentation; LDH; Lactate.
Subjects:	Natural sciences > Cell and molecular biology
Depositing User:	Eilish McLaughlin
Date Deposited:	13 Jun 2024 14:15
Last Modified:	13 Jun 2024 14:15
URI:	https://repository.uwl.ac.uk/id/eprint/12057

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