@article {712,
	title = {Storage of an Excess Proton in the Hydrogen-bonded Network of the D-pathway of Cytochrome c Oxidase: Identification of a Protonated Water Cluster},
	journal = {J Am Chem Soc},
	volume = {129},
	number = {10},
	year = {2007},
	note = {Xu, Jiancong Sharpe, Martyn A Qin, Ling Ferguson-Miller, Shelagh Voth, Gregory A GM053148/GM/NIGMS NIH HHS/United States GM26916/GM/NIGMS NIH HHS/United States R01 GM053148-05/GM/NIGMS NIH HHS/United States R01 GM053148-13/GM/NIGMS NIH HHS/United States R37 GM026916-29/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural United States Journal of the American Chemical Society J Am Chem Soc. 2007 Mar 14;129(10):2910-3. Epub 2007 Feb 20.},
	pages = {2910-3},
	abstract = {<p>The mechanism of proton transport in the D-pathway of cytochrome c oxidase (CcO) is further elucidated through examining a protonated water/hydroxyl cluster inside the channel. The second generation multi-state empirical valence bond (MS-EVB2) model was employed in a molecular dynamics study based on a high-resolution X-ray structure to simulate the interaction of the excess proton with the channel environment. Our results indicate that a hydrogen-bonded network consisting of about 5 water molecules surrounded by three side chains and two backbone groups (S197, S200, S201, F108) is involved in storage and translocation of an excess proton to the extracellular side of CcO.</p>},
	keywords = {Computer Simulation Electron Transport Complex IV/*chemistry/metabolism Hydrogen Bonding Models, Molecular Molecular Structure *Protons Rhodobacter sphaeroides/enzymology Water/*chemistry},
	doi = {10.1021/ja067360s},
	url = { },
	author = {Xu, J. and Sharpe, M. A. and Qin, L. and Ferguson-Miller, S. and G. A. Voth}
}
