X-ray crystal structure of the light-independent protochlorophyllide reductase

Norifumi Muraki, Jiro Nomata, Kozue Ebata, Tadashi Mizoguchi, Tomoo Shiba, Hitoshi Tamiaki, Genji Kurisu () and Yuichi Fujita ()
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Norifumi Muraki: University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan
Jiro Nomata: Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
Kozue Ebata: Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
Tadashi Mizoguchi: Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan
Tomoo Shiba: University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan
Hitoshi Tamiaki: Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan
Genji Kurisu: Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan
Yuichi Fujita: Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan

Nature, 2010, vol. 465, issue 7294, 110-114

Abstract: Dark greening materials Some photosynthetic organisms — pine seedlings and other gymnosperms for instance — are capable of 'greening' in the dark, in contrast to the strict requirement of light for the greening of angiosperm seedlings such as peas. The enzyme behind this dark art is dark-operative protochlorophyllide (Pchlide) oxidoreductase (DPOR), which catalyses the stereospecific reduction of the C17=C18 double bond of Pchlide to form chlorophyllide a, the direct precursor of chlorophyll a. The crystal structure of the NB-protein component of DPOR from the purple phototrophic bacterium Rhodobacter capsulatus has now been determined. The structure suggests a possible chemical mechanism by which the reduction of the C17=C18 double bond of Pchlide may occur. And interestingly, DPOR resembles the well-known nitrogen-fixing enzyme nitrogenase, suggesting a close evolutionary relationship between molecular mechanisms for nitrogen fixation and producing chlorophylls in the dark.

Date: 2010
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DOI: 10.1038/nature08950

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