Conferencia invitada en el simposio: Quantum-classical calculations in Chemistry and BiophysicsQM-MM investigation of chemical reactivity of heme proteins

D. A. ESTRIN

Filadelfia

Congreso; 228th National Meeting; 2004

American Chemical Society

QM-MM investigation of chemical reactivity of heme proteinsThe investigation of heme proteins is of interest due totheir widespread occurrence among diverse species as well as to their multiple and/or still unexplained functions. Due to the fact that chemical reactivity of these systems is subtly  modulated by their protein environment, a proper description requires a QM-MM treatment. We have developed a scheme  in which the active site is treated at the DFT level, as implemented in the efficient Siesta code,  while the rest of the protein is treated using the Amber force field parametrization. We will report results of our investigation of the following subjects:(i) reaction mechanism of nitrite reduction to NO in nitrite reductase of pseudomonas aeruginosa.(ii) nitric oxide trans effects in cytochrome c´ of Alcalignes xylosoxidans.(iii) nitric oxide detoxification mechanisms in truncated hemoglobins of mycobacterium tuberculosis.