Chlorophyllide a oxidoreductase Preferentially Catalyzes 8-Vinyl Reduction over B-Ring Reduction of 8-Vinyl Chlorophyllide a in the Late Steps of Bacteriochlorophyll Biosynthesis |
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Authors: | Dr Haruki Yamamoto Dr Tadashi Mizoguchi Dr Yusuke Tsukatani Prof Hitoshi Tamiaki Prof Genji Kurisu Prof Yuichi Fujita |
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Affiliation: | 1. Graduate School of Bioagricultural Sciences, Nagoya University Furo-cho, Chikusa-ku, Nagoya, 464-8601 Japan;2. Graduate School of Life Sciences, Ritsumeikan University Kusatsu, Shiga, 525-8577 Japan;3. Institute for Extra-cutting-edge Science and Technology Avant-garde Research (X-star), Japan Agency for Marine-Earth Science and Technology (JAMSTEC) Yokosuka, Kanagawa, 237-0061 Japan;4. Institute for Protein Research, Osaka University Suita, Osaka, 565-0871 Japan |
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Abstract: | Bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA, and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. Recently, we discovered 8VR activity in COR. However, the kinetic parameters of the COR 8VR activity remain unknown, while those of the COR C7=C8 reductase activity and BciA have been reported. Here, we determined the kinetic parameters of COR 8VR activity by using 8 V-Chlide. The Km value for 8 V-Chlide was 1.4 μM, which is much lower than the 6.2 μM determined for the C7=C8 reduction of Chlide. The kinetic parameters of the dual activities of COR suggest that COR catalyzes the reduction of the C8 vinyl group of 8 V-Chlide preferentially over C7=C8 reduction when both substrates are supplied during BChl biosynthesis. |
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Keywords: | bacteriochlorophyll biosynthesis chlorophyllide a oxidoreductase Rhodobacter capsulatus bciA bchXYZ |
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