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The Active Site Loop Modulates the Reorganization Energy of Blue Copper Proteins by Controlling the Dynamic Interplay with Solvent (Articolo in rivista)

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The Active Site Loop Modulates the Reorganization Energy of Blue Copper Proteins by Controlling the Dynamic Interplay with Solvent (Articolo in rivista) (literal)

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Paltrinieri L. [ 1 ] ; Borsari M. [ 1 ] ; Ranieri A. [ 2 ] ; Battistuzzi G. [ 1 ] ; Corni S. [ 3 ] ; Bortolotti C. A. [ 2,3 ] (2013)
The Active Site Loop Modulates the Reorganization Energy of Blue Copper Proteins by Controlling the Dynamic Interplay with Solvent
in The journal of physical chemistry letters; AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Paltrinieri L. [ 1 ] ; Borsari M. [ 1 ] ; Ranieri A. [ 2 ] ; Battistuzzi G. [ 1 ] ; Corni S. [ 3 ] ; Bortolotti C. A. [ 2,3 ] (literal)

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[ 1 ] Univ Modena & Reggio Emilia, Dept Chem & Geol Sci, I-41125 Modena, Italy [ 2 ] Univ Modena & Reggio Emilia, Dept Life Sci, I-41125 Modena, Italy [ 3 ] CNR Nano Inst Nanosci, I-41125 Modena, Italy (literal)

Titolo

The Active Site Loop Modulates the Reorganization Energy of Blue Copper Proteins by Controlling the Dynamic Interplay with Solvent (literal)

Abstract

Understanding the factors governing the rate of electron transfer processes in proteins is crucial not only to a deeper understanding of redox processes in living organisms but also for the design of efficient devices featuring biological molecules. Here, molecular dynamics simulations performed on native azurin and four chimeric cupredoxins allow for the calculation of the reorganization energy and of structure related quantities that were used to clarify the molecular determinants to the dynamics/function relationship in blue copper proteins. We find that the dynamics of the small, metal binding loop region controls the outer sphere reorganization energy not only by determining the exposure of the active site to solvent but also through the modulation of the redox-dependent rearrangement of the whole protein scaffold and of the surrounding water molecules. (literal)

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