@article {Ma2014c,
	title = {Rigid- and Polarizable-ion Potentials for Modeling Ru-polyoxometalate Catalysts for Water Oxidation},
	journal = {Acta chimica slovenica (Print ed.)},
	volume = {61},
	year = {2014},
	pages = {302–307},
	publisher = {Slovensko kemijsko drutvo.},
	address = {Ljubljana},
	abstract = {This work assesses the predictive power and capabilities of classical interatomic potentials for describing the atomistic structure of a fully inorganic water-oxidation catalyst in the gas phase and in solution. We address a Ru-polyoxometalate molecule (Ru-POM) that is presently one of the most promising catalysts for water oxidation due to its efficiency and stability under reaction conditions. The Ru-POM molecule is modeled with two interatomic potentials, the rigid ion model and the shell model potentials, which are used to perform molecular dynamics simulations. The predictions of these two approaches are discussed and compared to the available ab-initio data. These results allow us to establish the suitable level of theory to model complex heterogeneous interfaces between the Ru-POM and electrodes in solution.},
	keywords = {Artificial photosynthesis, homogeneous catalysis, Molecular dynamics simulations, polarizable interatomic potentials},
	issn = {1318-0207},
	author = {Ma, Changru and Piccinin, Simone and Fabris, Stefano}
}
@article {G.2014c,
	title = {Structure/function/dynamics of Photosystem II plastoquinone binding sites},
	journal = {Current protein and peptide science (Print)},
	volume = {15},
	year = {2014},
	pages = {285–295},
	publisher = {Bentham Science Publishers},
	address = {Hilversum},
	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. Â© 2014 Bentham Science Publishers.},
	keywords = {Molecular docking, Molecular dynamics simulations, Photosystem II, Plastoquinone, Plastoquinone binding site, Protein dynamics},
	issn = {1389-2037},
	doi = {10.2174/1389203715666140327104802},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84904459673&partnerID=q2rCbXpz},
	author = {Lambreva, M.D. and Russo, D. and Polticelli, F. and Scognamiglio, V. and Antonacci, A. and Zobnina, V. and Campi ,G. and Rea, G.}
}
