PMID- 22197476
OWN - NLM
STAT- MEDLINE
DCOM- 20120705
LR  - 20131121
IS  - 1873-3344 (Electronic)
IS  - 0162-0134 (Linking)
VI  - 108
DP  - 2012 Mar
TI  - Comparative studies in series of cytochrome c oxidase models.
PG  - 196-202
LID - 10.1016/j.jinorgbio.2011.11.016 [doi]
AB  - This study compares the behavior as cytochrome c oxidase (CcO) functional and 
      structural models of a series of reported and unreported ligands that provide 
      either a binding site for copper without a built-in proximal base, or both a 
      flexible binding site for copper and a built-in proximal base, or a fixed binding 
      site for copper with a built-in proximal base. The comparisons of the models show 
      that the relative position of the two metal sites is not only a crucial parameter 
      in the control of the catalytic behavior but also essential in mimicking other 
      features of the enzyme such as CO exchange between the ferrous heme a(3) and the 
      cuprous Cu(B) center.
CI  - Copyright A(c) 2011 Elsevier Inc. All rights reserved.
FAU - Melin, F
AU  - Melin F
AD  - Spectroscopie vibrationnelle et electrochimie des biomolecules, Institut de 
      Chimie de Strasbourg, UMR 7177 CNRS, Universite de Strasbourg, Strasbourg, 
      France. fmelin@unistra.fr
FAU - Trivella, A
AU  - Trivella A
FAU - Lo, M
AU  - Lo M
FAU - Ruzie, C
AU  - Ruzie C
FAU - Hijazi, I
AU  - Hijazi I
FAU - Oueslati, N
AU  - Oueslati N
FAU - Wytko, J A
AU  - Wytko JA
FAU - Boitrel, B
AU  - Boitrel B
FAU - Boudon, C
AU  - Boudon C
FAU - Hellwig, P
AU  - Hellwig P
FAU - Weiss, J
AU  - Weiss J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20111201
PL  - United States
TA  - J Inorg Biochem
JT  - Journal of inorganic biochemistry
JID - 7905788
RN  - 0 (Metals)
RN  - 42VZT0U6YR (Heme)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Binding Sites
MH  - Copper/chemistry
MH  - Electrochemistry/methods
MH  - Electron Transport Complex IV/*chemistry/*metabolism
MH  - Heme/chemistry
MH  - Metals/chemistry
EDAT- 2011/12/27 06:00
MHDA- 2012/07/06 06:00
CRDT- 2011/12/27 06:00
PHST- 2011/07/22 00:00 [received]
PHST- 2011/11/17 00:00 [revised]
PHST- 2011/11/20 00:00 [accepted]
PHST- 2011/12/27 06:00 [entrez]
PHST- 2011/12/27 06:00 [pubmed]
PHST- 2012/07/06 06:00 [medline]
AID - S0162-0134(11)00352-7 [pii]
AID - 10.1016/j.jinorgbio.2011.11.016 [doi]
PST - ppublish
SO  - J Inorg Biochem. 2012 Mar;108:196-202. doi: 10.1016/j.jinorgbio.2011.11.016. Epub 
      2011 Dec 1.