PMID- 22086149
OWN - NLM
STAT- MEDLINE
DCOM- 20120510
LR  - 20211021
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1817
IP  - 4
DP  - 2012 Apr
TI  - Coupled electron and proton transfer reactions during the O-->E transition in 
      bovine cytochrome c oxidase.
PG  - 506-17
LID - 10.1016/j.bbabio.2011.10.013 [doi]
AB  - A combined DFT/electrostatic approach is employed to study the coupling of proton 
      and electron transfer reactions in cytochrome c oxidase (CcO) and its proton 
      pumping mechanism. The coupling of the chemical proton to the internal electron 
      transfer within the binuclear center is examined for the O-->E transition. The 
      novel features of the His291 pumping model are proposed, which involve timely 
      well-synchronized sequence of the proton-coupled electron transfer reactions. The 
      obtained pK(a)s and E(m)s of the key ionizable and redox-active groups at the 
      different stages of the O-->E transition are consistent with available experimental 
      data. The PT step from E242 to H291 is examined in detail for various redox 
      states of the hemes and various conformations of E242 side-chain. Redox potential 
      calculations of the successive steps in the reaction cycle during the O-->E 
      transition are able to explain a cascade of equilibria between the different 
      intermediate states and electron redistribution between the metal centers during 
      the course of the catalytic activity. All four electrometric phases are discussed 
      in the light of the obtained results, providing a robust support for the His291 
      model of proton pumping in CcO.
CI  - Copyright A(c) 2011 Elsevier B.V. All rights reserved.
FAU - Popovic, Dragan M
AU  - Popovic DM
AD  - Department of Chemistry, University of California, Davis, CA, USA. 
      dpopovic@ucdavis.edu
FAU - Stuchebrukhov, Alexei A
AU  - Stuchebrukhov AA
LA  - eng
GR  - R01 GM054052/GM/NIGMS NIH HHS/United States
GR  - R29 GM054052/GM/NIGMS NIH HHS/United States
GR  - GM054052/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Review
DEP - 20111106
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Protons)
RN  - 4QD397987E (Histidine)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Biological Transport
MH  - Cattle
MH  - *Electron Transport
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Histidine/chemistry/metabolism
MH  - Kinetics
MH  - Models, Chemical
MH  - Models, Molecular
MH  - Oxidation-Reduction
MH  - *Protein Structure, Tertiary
MH  - *Protons
PMC - PMC4220735
MID - NIHMS337407
EDAT- 2011/11/17 06:00
MHDA- 2012/05/11 06:00
PMCR- 2014/11/05
CRDT- 2011/11/17 06:00
PHST- 2011/08/16 00:00 [received]
PHST- 2011/10/27 00:00 [revised]
PHST- 2011/10/29 00:00 [accepted]
PHST- 2011/11/17 06:00 [entrez]
PHST- 2011/11/17 06:00 [pubmed]
PHST- 2012/05/11 06:00 [medline]
PHST- 2014/11/05 00:00 [pmc-release]
AID - S0005-2728(11)00258-1 [pii]
AID - 10.1016/j.bbabio.2011.10.013 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2012 Apr;1817(4):506-17. doi: 10.1016/j.bbabio.2011.10.013. 
      Epub 2011 Nov 6.