期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY
卷 353, 期 -, 页码 661-666出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotochem.2017.09.010
关键词
Bacteriochlorophyll; BciA; Chlorophyllide oxidoreductase; Pigment biosynthesis; Photosynthesis
资金
- JSPS KAKENHI [JP15H00886, JP16K14907, JP17H05731, JP26102543, JP16H00784, JP26840099, JP17H05231, JP24107002]
- Grants-in-Aid for Scientific Research [17H05231, 16K14907, 17H05731] Funding Source: KAKEN
Divinyl-chlorophyllide a (DV-Chlide a) is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms. Previous mutational analyses revealed that BciA works for reduction of the C8-vinyl group of DV-Chlide a. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of Chlide a bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of DV-Chlide a. In this study, we prepared a recombinant BciA protein from the purple photosynthetic bacterium Rhodobacter capsulatus and analyzed its C8-vinyl reduction activity towards DV-Chlide a. BciA formed a functional oligomeric complex consisting of at least three rigid dimers. BciA required NADPH as an electron donor for its C8-vinyl reduction activity. The enzymatic activity of BciA towards the substrate DV-Chlide a was much higher than that of COR towards Chlide a. Phylogenetic distribution and the enzymatic parameters of BciA and COR suggest that BciA is a more recently acquired auxiliary C8-vinyl reductase, attained to meet the high demand for bacteriochlorophylls used to produce large amounts of light-harvesting complexes. (C) 2017 Elsevier B.V. All rights reserved.
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