Sulfur ligation in copper enzymes and models.
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.
Belle
Catherine
C
Laboratoire d'Etudes Dynamiques et Structurales de la Sélectivité, (Chimie Biomimétique, UMR CNRS 5616), ICMG FR CNRS 2607, Université Joseph Fourier, BP 53X, 38041 Grenoble Cedex 9, France. catherine.belle@ujf-grenoble.fr
Rammal
Wassim
W
Pierre
Jean-Louis
JL
D040761:Biomimetic Materials; D003300:Copper / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000378:metabolism; D004583:Electrons; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D005609:Free Radicals; D008024:Ligands; D008956:Models, Chemical; D010088:Oxidoreductases / Q000737:chemistry; D013455:Sulfur / Q000737:chemistry* / Q000378:metabolism*
D004798:Enzymes; D005609:Free Radicals; D008024:Ligands; D013455:Sulfur; D003300:Copper; D010088:Oxidoreductases; C022763:nitrous oxide reductase; D003576:Electron Transport Complex IV