Literature DB >> 21377371

Enzymatic function of cytochrome b559 in photosystem II.

Pavel Pospíšil1.   

Abstract

Cytochrome b(559) (cyt b(559)) is a heme-bridged protein heterodimer in photosystem II (PSII) of all oxygenic photosynthetic organisms. In spite of the fact that cyt b(559) is strictly required for proper function of PSII, it is not involved in the linear electron transport chain from water to plastoquinone. Instead of that the participation of cyt b(559) in the cyclic electron transport around PSII has been proposed mainly based on the ability of the heme iron to accept and donate an electron form the electron acceptor and to the electron donor side of PSII, respectively. In addition to the involvement of cyt b(559) in the cyclic electron transport around PSII, several lines of evidence have been provided on the enzymatic function of cyt b(559). The ability of oxygenic photosynthetic organisms to oxidize water and reduce plastoquinone is connected to the formation of reactive oxygen species (ROS) and thus required to develop an effective antioxidant defense system against ROS. The review attempts to summarize a recent progress on the role of cyt b(559) as oxygen reductase, superoxide reductase, superoxide oxidase and plastoquinol oxidase. The focus is mainly given on the characterization of redox, redox potential and acid-base properties of the heme iron in the putative enzymatic cycles. The possible oxidase and reductase enzymatic activity of cyt b(559) in protection from photoinhibition is discussed.
Copyright © 2011 Elsevier B.V. All rights reserved.

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Year:  2011        PMID: 21377371     DOI: 10.1016/j.jphotobiol.2011.02.013

Source DB:  PubMed          Journal:  J Photochem Photobiol B        ISSN: 1011-1344            Impact factor:   6.252


  19 in total

1.  Probing the N-terminal sequence of spinach PsbO: evidence that essential threonine residues bind to different functional sites in eukaryotic photosystem II.

Authors:  Hana Popelka; Charles Yocum
Journal:  Photosynth Res       Date:  2012-05-22       Impact factor: 3.573

2.  Towards an understanding of the nature of the redox forms of cytochrome b559 in photosystem II.

Authors:  O P Kaminskaya; V A Shuvalov
Journal:  Dokl Biochem Biophys       Date:  2013-07-04       Impact factor: 0.788

Review 3.  Photosynthesis-related quantities for education and modeling.

Authors:  Taras K Antal; Ilya B Kovalenko; Andrew B Rubin; Esa Tyystjärvi
Journal:  Photosynth Res       Date:  2013-10-26       Impact factor: 3.573

4.  Influence of thylakoid membrane lipids on the structure and function of the plant photosystem II core complex.

Authors:  Marcel Kansy; Christian Wilhelm; Reimund Goss
Journal:  Planta       Date:  2014-07-26       Impact factor: 4.116

5.  Consequences of structural modifications in cytochrome b559 on the electron acceptor side of Photosystem II.

Authors:  Makoto Nakamura; Alain Boussac; Miwa Sugiura
Journal:  Photosynth Res       Date:  2018-05-19       Impact factor: 3.573

6.  Antimycin A inhibits cytochrome b559-mediated cyclic electron flow within photosystem II.

Authors:  Daisuke Takagi; Kentaro Ifuku; Taishi Nishimura; Chikahiro Miyake
Journal:  Photosynth Res       Date:  2018-05-22       Impact factor: 3.573

7.  Control of STN7 transcript abundance and transient STN7 dimerisation are involved in the regulation of STN7 activity.

Authors:  Tobias Wunder; Qiuping Liu; Elena Aseeva; Vera Bonardi; Dario Leister; Mathias Pribil
Journal:  Planta       Date:  2012-10-21       Impact factor: 4.116

Review 8.  Molecular mechanisms for generating transmembrane proton gradients.

Authors:  M R Gunner; Muhamed Amin; Xuyu Zhu; Jianxun Lu
Journal:  Biochim Biophys Acta       Date:  2013-03-16

9.  Study of the nature of biphasic reduction of cytochrome b559 by plastoquinol in photosystem II membrane fragments.

Authors:  O P Kaminskaya; L G Erokhina; V A Shuvalov
Journal:  Dokl Biochem Biophys       Date:  2013-01-04       Impact factor: 0.788

10.  Towards an understanding of redox heterogeneity of the photosystem II cytochrome b559 in the native membrane.

Authors:  Olga P Kaminskaya; Vladimir A Shuvalov
Journal:  Eur Biophys J       Date:  2015-10-07       Impact factor: 1.733

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