Structure/Function/Dynamics of Photosystem II Plastoquinone Binding Sites

ISSN: 1875-5550 (Online)
ISSN: 1389-2037 (Print)


Volume 15, 8 Issues, 2014


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Current Protein & Peptide Science

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Structure/Function/Dynamics of Photosystem II Plastoquinone Binding Sites

Author(s): Maya D. Lambreva, Daniela Russo, Fabio Polticelli, Viviana Scognamiglio, Amina Antonacci, Veranika Zobnina, Gaetano Campi and Giuseppina Rea

Affiliation: Institute of Crystallography, National Research Council, Monterotondo, Italy.

Abstract

Photosystem II (PSII) continuously attracts the attention of researchers aiming to unravel the riddle of its functioning and efficiency fundamental for all life on Earth. Besides, an increasing number of biotechnological applications have been envisaged exploiting and mimicking the unique properties of this macromolecular pigment-protein complex. The PSII organization and working principles have inspired the design of electrochemical water splitting schemes and charge separating triads in energy storage systems as well as biochips and sensors for environmental, agricultural and industrial screening of toxic compounds. An intriguing opportunity is the development of sensor devices, exploiting native or manipulated PSII complexes or ad hoc synthesized polypeptides mimicking the PSII reaction centre proteins as biosensing elements. This review offers a concise overview of the recent improvements in the understanding of structure and function of PSII donor side, with focus on the interactions of the plastoquinone cofactors with the surrounding environment and operational features. Furthermore, studies focused on photosynthetic proteins structure/function/dynamics and computational analyses aimed at rational design of high-quality bio-recognition elements in biosensor devices are discussed.

Keywords: Molecular docking, molecular dynamics simulations, Photosystem II, plastoquinone, plastoquinone binding site, protein dynamics.

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Article Details

Volume: 15
Issue Number: 4
First Page: 285
Last Page: 295
Page Count: 11
DOI: 10.2174/1389203715666140327104802
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