@article {713,
	title = {Computer Simulation of Explicit Proton Translocation in Cytochrome c Oxidase: the D-pathway},
	journal = {Proc Natl Acad Sci U S A},
	volume = {102},
	number = {19},
	year = {2005},
	note = {Xu, Jiancong Voth, Gregory A R01 GM053148/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, U.S. Gov{\textquoteright}t, P.H.S. United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2005 May 10;102(19):6795-800. Epub 2005 Apr 27.},
	pages = {6795-800},
	abstract = {<p>Proton translocation in the D-pathway of cytochrome c oxidase has been studied by a combination of classical molecular dynamics and the multistate empirical valence bond methodology. This approach allows for explicit Grotthuss proton hopping between water molecules. According to mutagenesis experiments, the role of proton donor/acceptor along the D-pathway is carried by the highly conserved residue Glu-242. The present multistate empirical valence bond simulations indicate that the protonation/deprotonation state of Glu-242 is strongly coupled to the distance of proton propagation in the D-pathway. The proton was seen to travel the full length of the D-pathway when Glu-242 was deprotonated; however, it was trapped halfway along the path when Glu-242 was protonated. Further investigation in terms of both proton dynamical properties and free energy calculations for the pathway of proton transport provides evidence for a two-step proton transport mechanism in the D-pathway.</p>},
	keywords = {Animals Biophysics/*methods Cattle Computer Simulation Crystallography, Molecular Models, Statistical Mutagenesis Protons Serine/chemistry Static Electricity Thermodynamics Time Factors Water/chemistry, X-Ray Electron Transport Complex IV/*chemistry Glutamic Acid/chemistry Mitochondria/metabolism Models},
	doi = {10.1073/pnas.0408117102},
	author = {Xu, J. and G. A. Voth}
}
