PMID- 16051368
OWN - NLM
STAT- MEDLINE
DCOM- 20051201
LR  - 20131121
IS  - 0162-0134 (Print)
IS  - 0162-0134 (Linking)
VI  - 99
IP  - 10
DP  - 2005 Oct
TI  - Sulfur ligation in copper enzymes and models.
PG  - 1929-36
AB  - Biological copper-sulfur entities display versatile and unusual coordination 
      chemistry. The role of the sulfur ligation is briefly reviewed through examples 
      from selected copper enzymes and relevant biomimetic models. Copper thiolate 
      complexes are of particular interest because of their key roles in a number of 
      ubiquitous metalloenzymes such as Type I (blue copper proteins) or in the 
      binuclear Cu(A) electrons transfer site found in both cytochrome c oxidase (CcO) 
      and nitrous oxide reductase (N2OR). The possible roles of the S(Met) ligand in 
      monoxygenases are described in relation to recently proposed pathways. Some 
      prospective regarding the biological relevance of disulfide copper ligation and 
      possible radical copper bonds in catalytic cycle are also discussed.
FAU - Belle, Catherine
AU  - Belle C
AD  - Laboratoire d'Etudes Dynamiques et Structurales de la Selectivite, (Chimie 
      Biomimetique, UMR CNRS 5616), ICMG FR CNRS 2607, Universite Joseph Fourier, BP 
      53X, 38041 Grenoble Cedex 9, France. catherine.belle@ujf-grenoble.fr
FAU - Rammal, Wassim
AU  - Rammal W
FAU - Pierre, Jean-Louis
AU  - Pierre JL
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - J Inorg Biochem
JT  - Journal of inorganic biochemistry
JID - 7905788
RN  - 0 (Enzymes)
RN  - 0 (Free Radicals)
RN  - 0 (Ligands)
RN  - 70FD1KFU70 (Sulfur)
RN  - 789U1901C5 (Copper)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.7.2.4 (nitrous oxide reductase)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Biomimetic Materials
MH  - Copper/*chemistry
MH  - Electron Transport Complex IV/metabolism
MH  - Electrons
MH  - Enzymes/chemistry/*metabolism
MH  - Free Radicals
MH  - Ligands
MH  - *Models, Chemical
MH  - Oxidoreductases/chemistry
MH  - Sulfur/*chemistry/*metabolism
RF  - 59
EDAT- 2005/07/30 09:00
MHDA- 2005/12/13 09:00
CRDT- 2005/07/30 09:00
PHST- 2005/05/02 00:00 [received]
PHST- 2005/06/13 00:00 [revised]
PHST- 2005/06/15 00:00 [accepted]
PHST- 2005/07/30 09:00 [pubmed]
PHST- 2005/12/13 09:00 [medline]
PHST- 2005/07/30 09:00 [entrez]
AID - S0162-0134(05)00175-3 [pii]
AID - 10.1016/j.jinorgbio.2005.06.013 [doi]
PST - ppublish
SO  - J Inorg Biochem. 2005 Oct;99(10):1929-36. doi: 10.1016/j.jinorgbio.2005.06.013.