TY - JOUR
T1 - Electron transfer pathways in cytochrome c oxidase
AU - Lucas, M. Fátima
AU - Rousseau, Denis L.
AU - Guallar, Victor
N1 - Funding Information:
Computational resources were provided by the Barcelona Supercomputing Center. Work was supported by funds from the Barcelona Supercomputer Center and through the Spanish Ministry of Education and Science through the project CTQ2007-62122/BQU. MFL was supported by The Fundação para a Ciência e Tecnologia —grant SFRH/BPD/47901/2008 . DLR is supported by NIH Grant GM074982 .
PY - 2011/10
Y1 - 2011/10
N2 - Mixed quantum mechanical/molecular mechanics calculations were used to explore the electron pathway of the terminal electron transfer enzyme, cytochrome c oxidase. This enzyme catalyzes the reduction of molecular oxygen to water in a multiple step process. Density functional calculations on the three redox centers allowed for the characterization of the electron transfer mechanism, following the sequence CuA → heme a → heme a3. This process is largely affected by the presence of positive charges, confirming the possibility of a proton coupled electron transfer. An extensive mapping of all residues involved in the electron transfer, between the CuA center (donor) and the O2 reduction site heme a 3-CuB (receptor), was obtained by selectively activating/deactivating different quantum regions. The method employed, called QM/MM e-pathway, allowed the identification of key residues along the possible electron transfer paths, consistent with experimental data. In particular, the role of arginines 481 and 482 appears crucial in the CuA → heme a and in the heme a → heme a3 electron transfer processes. This article is part of a Special Issue entitled: Allosteric cooperativity in respiratory proteins.
AB - Mixed quantum mechanical/molecular mechanics calculations were used to explore the electron pathway of the terminal electron transfer enzyme, cytochrome c oxidase. This enzyme catalyzes the reduction of molecular oxygen to water in a multiple step process. Density functional calculations on the three redox centers allowed for the characterization of the electron transfer mechanism, following the sequence CuA → heme a → heme a3. This process is largely affected by the presence of positive charges, confirming the possibility of a proton coupled electron transfer. An extensive mapping of all residues involved in the electron transfer, between the CuA center (donor) and the O2 reduction site heme a 3-CuB (receptor), was obtained by selectively activating/deactivating different quantum regions. The method employed, called QM/MM e-pathway, allowed the identification of key residues along the possible electron transfer paths, consistent with experimental data. In particular, the role of arginines 481 and 482 appears crucial in the CuA → heme a and in the heme a → heme a3 electron transfer processes. This article is part of a Special Issue entitled: Allosteric cooperativity in respiratory proteins.
KW - Bioenergetics
KW - Cytochrome c oxidase
KW - Electron transfer
KW - QM/MM e-pathway
KW - heme
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U2 - 10.1016/j.bbabio.2011.03.003
DO - 10.1016/j.bbabio.2011.03.003
M3 - Article
C2 - 21419097
AN - SCOPUS:80051594329
SN - 0005-2728
VL - 1807
SP - 1305
EP - 1313
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 10
ER -