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Role of the electronic properties of azurin active site in the electron‐transfer process
Author(s) -
Corni Stefano,
De Rienzo Francesca,
Di Felice Rosa,
Molinari Elisa
Publication year - 2004
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.20374
Subject(s) - azurin , electron transfer , copper protein , chemistry , electronic structure , redox , density functional theory , wave function , electron , chemical physics , active site , copper , atomic physics , computational chemistry , inorganic chemistry , physics , quantum mechanics , biochemistry , enzyme , organic chemistry
Abstract Electron transfer proteins, such as azurin (a blue copper protein), are promising candidates for the implementation of biomolecular nanoelectronic devices. To understand the details of electron transfer in redox active azurin molecules, we performed plane‐wave pseudo‐potential density functional theory (DFT) calculations of the protein active site in the two possible oxidation states Cu(I) and Cu(II). The ab initio results are used to discuss how the electronic spectrum and wavefunctions may mediate the shuttling of electrons through the copper ion. We find that the Cu‐ligand hybridization is very similar in the two charge states of the metal center, but the energy spectrum changes substantially. This result might indicate important effects of electronic correlations in the redox activity and consequent electron transfer through the Cu site. © 2004 Wiley Periodicals, Inc. Int J Quantum Chem, 2005