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Conformational fluctuations and electronic properties in myoglobin
Author(s) -
Aschi Massimiliano,
Zazza Costantino,
Spezia Riccardo,
Bossa Cecilia,
Di Nola Alfredo,
Paci Maurizio,
Amadei Andrea
Publication year - 2004
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20029
Subject(s) - myoglobin , biomolecule , electronic structure , chemical physics , hemeprotein , coupling (piping) , molecular dynamics , chemistry , heme , computational chemistry , materials science , biochemistry , organic chemistry , metallurgy , enzyme
In this article we use the recently developed perturbed matrix method (PMM) to investigate the effect of conformational fluctuations on the electronic properties of heme in Myoglobin. This widely studied biomolecule has been chosen as a benchmark for evaluating the accuracy of PMM in a large and complex system. Using a long, 80‐ns, molecular dynamics simulation and unperturbed Configuration Interaction (CISD) calculations in PMM, we reproduced the main spectroscopic features of deoxy‐Myoglobin. Moreover, in line with our previous results on a photosensitive protein, this study reveals a clear dynamical coupling between electronic properties and conformational fluctuations, suggesting that this correlation could be a general feature of proteins. © 2004 Wiley Periodicals, Inc. J Comput Chem 7: 974–984, 2004