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Published on August 20, 2008; 10.1104/pp.108.123117

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Received May 18, 2008
Accepted August 14, 2008

slr1923 of Synechocystis sp. PCC6803 is essential for conversion of 3,8-divinyl(proto)chlorophyll(ide) to 3-monovinyl(proto)chlorophyll(ide)

Md. Rafiqul Islam , Shimpei Aikawa , Takafumi Midorikawa , Yasuhiro Kashino , Kazuhiko Satoh , and Hiroyuki Koike *

Department of Life Science, Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan; Department of Life Sciences (Biology), The University of Tokyo, Komaba 3-8-1, Meguro, Tokyo, 153-8902, Japan

* Corresponding author; email: hkoike{at}bio.chuo-u.ac.jp.

The deduced amino acid sequence of an slr1923 gene of Synechocystis sp. PCC6803 is homologous to archaean F420H2 dehydrogenase, which acts as an soluble subcomplex of NADH dehydrogenase complex I. In the present study, the gene was inactivated and characteristics of the mutant were analyzed. The mutant grew slower than wild type under 100 µE m-2 s-1 but did not grow under high light intensity (300 µE m-2s-1). The cellular content of chlorophyll was lower in the mutant and absorption spectrum showed a shift in the absorption peak of the Soret band to longer wavelength by about 10 nm compared with wild type. It was found that retention time of chlorophyll of the mutant is shorter than wild type and peak wavelength of Soret band was also shifted to longer wavelength by 11 nm by HPLC analysis. 1H-NMR analysis of the chlorophyll of the mutant revealed that the ethyl group of position 8 of ring B is replaced with vinyl group. The spectrum indicates that the chlorophyll of the mutant is not a normal (3-vinyl) chlorophyll a but a 3,8-divinylchlorophyll a. These results strongly suggest that Slr1923 protein is essential to convert from divinyl-chlorophyll(ide) to normal chlorophyll(ide). We thus designate this gene as cvrA (a gene indispensable for cyanobacterial vinyl reductase).






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