http://www.cnr.it/ontology/cnr/individuo/prodotto/ID298546
Structure/function/dynamics of Photosystem II plastoquinone binding sites (Articolo in rivista)
- Type
- Label
- Structure/function/dynamics of Photosystem II plastoquinone binding sites (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.2174/1389203715666140327104802 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lambreva M.D.; Russo D.; Polticelli F.; Scognamiglio V.; Antonacci A.; Zobnina V.; Campi G.; Rea G. (literal)
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- Pagina fine
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-84904459673&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- Institute of Crystallography, National Research Council, Monterotondo, Italy; Istituto Officina dei Materiali, National Research Council, c/o Institut Laue-Langevin, Grenoble, France; Institut Lumière Matière, Université de Lyon 1, France; Department of Sciences, University Roma Tre, Rome, Italy; National Institute of Nuclear Physics, Roma Tre Section, Rome, Italy (literal)
- Titolo
- Structure/function/dynamics of Photosystem II plastoquinone binding sites (literal)
- 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. © 2014 Bentham Science Publishers. (literal)
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