PMID- 25135480
OWN - NLM
STAT- MEDLINE
DCOM- 20150108
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1847
IP  - 1
DP  - 2015 Jan
TI  - Infrared and Raman spectroscopic investigation of the reaction mechanism of 
      cytochrome c oxidase.
PG  - 86-97
LID - S0005-2728(14)00562-3 [pii]
LID - 10.1016/j.bbabio.2014.08.002 [doi]
AB  - Recent progress in studies on the proton-pumping and O(2)reduction mechanisms of 
      cytochrome c oxidase (CcO) elucidated by infrared (IR) and resonance Raman (rR) 
      spectroscopy, is reviewed. CcO is the terminal enzyme of the respiratory chain 
      and its O(2)reduction reaction is coupled with H(+) pumping activity across the inner 
      mitochondrial membrane. The former is catalyzed by heme a3 and its mechanism has 
      been determined using a rR technique, while the latter used the protein moiety 
      and has been investigated with an IR technique. The number of H(+) relative to e(-) 
      transferred in the reaction is 1:1, and their coupling is presumably performed by 
      heme a and nearby residues. To perform this function, different parts of the 
      protein need to cooperate with each other spontaneously and sequentially. It is 
      the purpose of this article to describe the structural details on the coupling on 
      the basis of the vibrational spectra of certain specified residues and 
      chromophores involved in the reaction. Recent developments in time-resolved IR 
      and Raman technology concomitant with protein manipulation methods have yielded 
      profound insights into such structural changes. In particular, the new IR 
      techniques that yielded the breakthrough are reviewed and assessed in detail. 
      This article is part of a Special Issue entitled: Vibrational spectroscopies and 
      bioenergetic systems.
CI  - Copyright (c) 2014. Published by Elsevier B.V.
FAU - Nakashima, Satoru
AU  - Nakashima S
AD  - Picobiology Institute, Graduate School of Life Science, University of Hyogo, 
      RSC-UH Leading Program Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, 
      Japan.
FAU - Ogura, Takashi
AU  - Ogura T
AD  - Picobiology Institute, Graduate School of Life Science, University of Hyogo, 
      RSC-UH Leading Program Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, 
      Japan; Department of Life Science, Graduate School of Life Science, University of 
      Hyogo, RSC-UH Leading Program Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 
      679-5148, Japan.
FAU - Kitagawa, Teizo
AU  - Kitagawa T
AD  - Picobiology Institute, Graduate School of Life Science, University of Hyogo, 
      RSC-UH Leading Program Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, 
      Japan. Electronic address: teizo@sci.u-hyogo.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20140816
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Proton Pumps)
RN  - 0 (Protons)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Electron Transport
MH  - Electron Transport Complex IV/*chemistry/*metabolism
MH  - Models, Molecular
MH  - Oxygen/chemistry/metabolism
MH  - Proton Pumps/chemistry/metabolism
MH  - Protons
MH  - Spectrophotometry, Infrared/methods
MH  - Spectrum Analysis, Raman/methods
OTO - NOTNLM
OT  - Cytochrome c oxidase
OT  - Proton-pumping mechanism
OT  - Time-resolved infrared and Raman spectroscopy
EDAT- 2014/08/20 06:00
MHDA- 2015/01/09 06:00
CRDT- 2014/08/20 06:00
PHST- 2014/04/28 00:00 [received]
PHST- 2014/07/07 00:00 [revised]
PHST- 2014/08/11 00:00 [accepted]
PHST- 2014/08/20 06:00 [entrez]
PHST- 2014/08/20 06:00 [pubmed]
PHST- 2015/01/09 06:00 [medline]
AID - S0005-2728(14)00562-3 [pii]
AID - 10.1016/j.bbabio.2014.08.002 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2015 Jan;1847(1):86-97. doi: 10.1016/j.bbabio.2014.08.002. 
      Epub 2014 Aug 16.