Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 45, Pages 15002-15021Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja803112w
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Funding
- USPHS [GM35342, GM39914, GM43278]
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A mechanism for proton pumping by the B-type cytochrome c oxidises is presented in which one proton is pumped in conjunction with the weakly exergonic, two-electron reduction of Fe-bound O-2 to the Fe-Cu bridging peroxodianion and three protons are pumped in conjunction with the highly exergonic, two-electron reduction of Fe(III)-O--O--Cu(II) to form water and the active oxidized enzyme, Fe(III)--OH,Cu(II). The scheme is based on the active-site structure of cytochrome ba(3) from Thermus thermophilus, which is considered to be both necessary and sufficient for coupled O-2 reduction and proton pumping when appropriate gates are in place (not included in the model). Fourteen detailed structures obtained from density functional theory (DFT) geometry optimization are presented that are reasonably thought to occur during the four-electron reduction of O-2. Each proton-pumping step takes place when a proton resides on the imidazole ring of I-His376 and the large active-site cluster has a net charge of +1 due to an uncompensated, positive charge formally associated with CUB. Four types of DFT were applied to determine the energy of each intermediate, and standard thermochemical approaches were used to obtain the reaction free energies for each step in the catalytic cycle. This application of DFT generally conforms with previously suggested criteria for a valid model (Siegbahn, P. E. M.; Blomberg, M. A. R. Chem. Rev. 2000, 100, 421-437) and shows how the chemistry of O-2 reduction in the heme a(3)-CUB dinuclear center can be harnessed to generate an electrochemical proton gradient across the lipid bilayer.
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