Thylakoid Membrane-Bound, NADPH-Specific Pyridine Nucleotide Dehydrogenase Complex Mediates Cyclic Electron Transport in the Cyanobacterium Synechocystis sp. PCC 6803 : PROTEINS, ENZYMES AND METABOLISM : MEMBRANES AND BIOENERGETICS

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概要

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• The donation of electrons from NADPH to the intersystem chain, as monitored by an increase in Chl fluorescence, occurred in the isolated thylakoid membranes of Synechocystis PCC 6803. The stimulation by NADPH of the methyl viologen-dependent photoreduction of dioxygen and of the reduction of P700^+ after photooxidation in the presence of DCMU also confirmed the donation of electrons from NADPH to the electron carriers in the intersystem. These reactions were sensitive to rotenone, capsaicin, 1-(2-thenoyl)-3,3,3-trifluoroacetone and HgCl_2 but not to antimycin A or flavone. In contrast to the thylakoid membranes from the wild type, those from a mutant, designated M55, in which a gene of a subunit of the pyridine nucleotide dehydrogenase complex (NDH) had been inactivated, did not show evidence of such reactions. These results sup-port our previous hypothesis that the transport of electrons from NADPH to the intersystem chain is mediated by NDH [Mi et al. (1994) Plant Cell Physiol. 35: 163] and indicate the binding of an NADPH-specific NDH to the thylakoid membranes. The Chl fluorescence was quenched transiently by addition of ferredoxin and NADP^+ to the thylakoid membranes but showed a sub-sequent increase. This result suggests the reduction of plastoquinone by the photoreduced NADP^+ and initiation of the NADPH-mediated cyclic flow of electrons around PSI. Further-more, a similar response of Chl fluorescence was observed upon the addition of ferredoxin only, demonstrating the ferredoxin-dependent cyclic flow of electrons. Both pathways of cyclic electron transport were inhibited by rotenone, and were not detected in the NDH-defected thylakoid membranes from M55, indicating the participation of the NDH complex. These results confirm that, in Synechocystis, the thylakoid-bound NDH complex mediates the ferredoxin-dependent cyclic electron flow, as well as the NADPH-dependent cyclic electron flow.

• 日本植物生理学会の論文

著者

• Asada Kozi

  Dept. Biotech Fac. Engin. Fukuyama Univ.

• Asada K

  The Research Institute For Food Science Kyoto University

• OGAWA Teruo

  Bioscience Center, Nagoya Univ.

• ENDO Tsuyoshi

  Kyoto Univ.Food Sci.

• Endo Tsuyoshi

  The Research Institute for Food Science, Kyoto University

• Asada Kozi

  The Research Institute for Food Science, Kyoto University

• MIHENDO Tualing

  The Research Institute for Food Science, Kyoto University

• Ogawa Teruo

  Bioscience Center Nagoya Univ.

• Ogawa T

  Nagoya Univ. Nagoya Jpn

• Asada Kozi

  The Research Institute For Food Science Kyoto University:(present)department Of Biotechnology Facult

• Endo Tsuyoshi

  Department Of Bioresource Science Obihiro University Of Agriculture And Veterinary Medicine

• Endo Tsuyoshi

  The Research Institute For Food Science Kyoto University

• Ogawa Teruo

  Biosci. Center Nagoya Univ.

• Endo Tsuyoshi

  Department Of Plant Genes And Totipotency Graduate School Of Biostudies Kyoto University

• Endo Tsuyoshi

  Division Of Applied Life Sciences Graduae School Of Agriculture

• Asada Kozi

  The Research Institute For Food Science Kyoto Niversity

• Endo T

  Graduate School Of Biostudies Kyoto University

• Asada Kozi

  The Research Institulefor Fbod Science Kyoto University

• Mihendo Tualing

  The Research Institute For Food Science Kyoto University

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