BibTex format

author = {Burgess, SJ and Hussein, T and Yeoman, JA and Iamshanova, O and Chan, KX and Boehm, M and Bundy, J and Bialek, W and Murray, JW and Nixon, PJ},
doi = {pcp/pcv167},
journal = {Plant and Cell Physiology},
pages = {82--94},
title = {Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts},
url = {},
volume = {57},
year = {2015}

RIS format (EndNote, RefMan)

AB - Under anoxic conditions the green alga Chlamydomonas reinhardtii activates various 67 fermentation pathways leading to the creation of formate, acetate, ethanol and small 68 amounts of other metabolites including D-lactate and hydrogen. Progress has been 69 made in identifying the enzymes involved in these pathways and their sub-cellular 70 locations; however, the identity of the enzyme involved in reducing pyruvate to D-71 lactate has remained unclear. Based on sequence comparisons, enzyme activity 72 measurements, X-ray crystallography, biochemical fractionation and analysis of 73 knock-down mutants we conclude that pyruvate reduction in the chloroplast is 74 catalysed by a tetrameric NAD-dependent D-lactate dehydrogenase encoded by 75 Cre07.g324550. Its expression during aerobic growth supports a possible function as a 76 ‘lactate valve’ for the export of lactate to the mitochondrion for oxidation by 77 cytochrome-dependent D-lactate dehydrogenases and by glycolate dehydrogenase. 78 We also present a revised spatial model of fermentation based on our 79 immunochemical detection of the likely pyruvate decarboxylase, PDC3, in the 80 cytoplasm.
AU - Burgess,SJ
AU - Hussein,T
AU - Yeoman,JA
AU - Iamshanova,O
AU - Chan,KX
AU - Boehm,M
AU - Bundy,J
AU - Bialek,W
AU - Murray,JW
AU - Nixon,PJ
DO - pcp/pcv167
EP - 94
PY - 2015///
SN - 1471-9053
SP - 82
TI - Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts
T2 - Plant and Cell Physiology
UR -
UR -
VL - 57
ER -