Cooperation of Photosynthetic Reaction Center of Photosystem II under Weak Light as Shown by Light Intensity-dependence of the Half-effective Dose of Atrazine

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概要

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• The binding constant (K) and number of binding sites (N) of atrazine to isolated photosystem (PS) II membranes were measured with an apparent correlation between N and the activity of oxygen evolution. Upon the addition of an electron acceptor, N became equal to the total number of the population of PS II reaction centers irrespective of having oxygen-evolving activity, about 4 mmol per mole of chlorophyll, with a concomitant decline of K from 1.32 (±0. 34)x10^7M^<-1> to 4.09 (±0.40)x10^6M^<-1>. NH_2OH and NaCl treatments, which inactivate oxygen evolution, affected neither the binding to PS II membranes of the extrinsic 33-kDa protein or of atrazine. The atrazine binding sites that are latent in CaCl_2-treated PS II membranes was partially restored by the reconstitution of the membranes with isolated extrinsic 33-kDa protein. An oxidizing system involving the 33-kDa protein may provide a suitable structure of PS II reaction center complex for atrazine binding. The level of inhibition of oxygen-evolving activity by atrazine under the saturating intensity of light parallels the fraction of the photosystem (PS) II reaction center with the quinone-binding site blocked by atrazine. In contrast, under a rate-limiting intensity of light, percents of remaining oxygen-evolving activity after the addition of atrazine correlated with the 1.33th power of the fraction of atrazine-free binding sites. Inhibition of PS II complexes more than one that bound with atrazine suggests a cooperation between PS II complexes to evolve oxygen under weak light intensity.

• 社団法人日本農芸化学会の論文
• 1995-05-23

著者

• Inoue Yuichi

  Second Department Of Surgery School Of Medicine University Of Occupational And Environmental Health

• Asada Kozi

  Research Institute for Food Science, Kyoto University

• Takahashi Masaaki

  Department of Pharmacy, National Hospital Organization Nagoya Medical Center

• Asada K

  Fukuyama Univ. Hiroshima Jpn

• Asada Kozi

  Dept. Biotech Fac. Engin. Fukuyama Univ.

• Asada K

  The Research Institute For Food Science Kyoto University

• Takano Masayoshi

  Department of Biology, Faculty of Science, Konan University

• Shiraishi Takuo

  Research Institute for Food Science, Kyoto University

• Inoue Yorinao

  Solar Energy Research Group, Institute for Physical and Chemical Research

• Asada Kozi

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

• Shiraishi Takuo

  Research Institute For Food Science Kyoto University

• TAKANO MASAYUKI

  Fine Chemicals Research Laboratories, Kaneka Corporation

• Inoue Y

  Showa Sangyo Co. Ltd.

• Inoue Y

  Solar Energy Research Group Institute For Physical And Chemical Research

• Inoue Yorinao

  Photosynthesis Research Lab.

• Takano Masayuki

  Fine Chemicals Research Laboratories Kaneka Corporation

• Asada Kozi

  Research Institute For Food Science Kyoto University

• Takahashi M

  Diagnostics Research And Development Department Asahi-kasei Corporation

• Takahashi Masaaki

  Department Of Orthopaedic Surgery Hamamatsu University School Of Medicine

• Inoue Yorinao

  Solar Energy Research Group Riken

• Takahashi Masaaki

  Department Of Applied Biological Sciences Graduate School Of Life And Environmental Sciences Osaka P

• Inoue Yorinao

  Solar Ener.res.group Riken

• Takahashi Masaaki

  Department Of Applied Biological Chemistry Faculty Of Agriculture Osaka Prefecture University

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