Journal article Open Access

# Theoretical description of protein field effects on electronic excitations of biological chromophores

Varsano, Daniele; Caprasecca, Stefano; Coccia, Stefano

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<foaf:name>Varsano, Daniele</foaf:name>
<foaf:givenName>Daniele</foaf:givenName>
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<foaf:name>Caprasecca, Stefano</foaf:name>
<foaf:givenName>Stefano</foaf:givenName>
<foaf:familyName>Caprasecca</foaf:familyName>
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<foaf:name>Dipartimento di Chimica e Chimica Industriale, Università di Pisa</foaf:name>
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<foaf:name>Coccia, Stefano</foaf:name>
<foaf:givenName>Stefano</foaf:givenName>
<foaf:familyName>Coccia</foaf:familyName>
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<foaf:name>Dipartimento di Scienze Fisiche e Chimiche, Università degli studi dell'Aquila</foaf:name>
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<dct:title>Theoretical description of protein field effects on electronic excitations of biological chromophores</dct:title>
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<dct:issued rdf:datatype="http://www.w3.org/2001/XMLSchema#gYear">2016</dct:issued>
<dcat:keyword>biological chromophore, ab initio, DFT, Quantum Monte Carlo, Many Body Perturbation Theory, QM/MM</dcat:keyword>
<dct:issued rdf:datatype="http://www.w3.org/2001/XMLSchema#date">2016-11-10</dct:issued>
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<dct:description>&lt;p&gt;Photoinitiated phenomena play a crucial role in many living organisms. Plants, algae, and bacteria absorb sunlight to perform photosynthesis, and convert water and carbon dioxide into molecular oxygen and carbohydrates, thus forming the basis for life on Earth. The vision of vertebrates is accomplished in the eye by a protein called rhodopsin, which upon photon absorption performs an ultrafast isomerisation of the retinal chromophore, triggering the signal cascade. Many other biological functions start with the photoexcitation of a protein-embedded pigment, followed by complex processes comprising, for example, electron or excitation energy transfer in photosynthetic complexes. The optical properties of chromophores in living systems are strongly dependent on the interaction with the surrounding environment (nearby protein residues, membrane, water), and the complexity of such interplay is, in most cases, at the origin of the functional diversity of the photoactive proteins. The specific interactions with the environment often lead to a significant shift of the chromophore excitation energies, compared with their absorption in solution or gas phase. The investigation of the optical response of chromophores is generally not straightforward, from both experimental and theoretical standpoints; this is due to the difficulty in understanding diverse behaviours and effects, occurring at different scales, with a single technique. In particular, the role played by &lt;em&gt;ab initio&lt;/em&gt; calculations in assisting and guiding experiments, as well as in understanding the physics of photoactive proteins, is fundamental. At the same time, owing to the large size of the systems, more approximate strategies which take into account the environmental effects on the absorption spectra are also of paramount importance. Here we review the recent advances in the first-principle description of electronic and optical properties of biological chromophores embedded in a protein environment. We show their applications on paradigmatic systems, such as the light-harvesting complexes, rhodopsin and green fluorescent protein, emphasising the theoretical frameworks which are of common use in solid state physics, and emerging as promising tools for biomolecular systems&lt;/p&gt;</dct:description>
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