Literature DB >> 15573156

Bio-mimicking galactose oxidase and hemocyanin, two dioxygen-processing copper proteins.

Patrick Gamez1, Iryna A Koval, Jan Reedijk.   

Abstract

The modelling of the active sites of metalloproteins is one of the most challenging tasks in bio-inorganic chemistry. Copper proteins form part of this stimulating field of research as copper enzymes are mainly involved in oxidation bio-reactions. Thus, the understanding of the structure-function relationship of their active sites will allow the design of effective and environmental friendly oxidation catalysts. This perspective illustrates some outstanding structural and functional synthetic models of the active site of copper proteins, with special attention given to models of galactose oxidase and hemocyanin.

Entities:  

Mesh:

Substances:

Year:  2004        PMID: 15573156     DOI: 10.1039/b413535k

Source DB:  PubMed          Journal:  Dalton Trans        ISSN: 1477-9226            Impact factor:   4.390


  2 in total

1.  Catecholase activity of a mu-hydroxodicopper(II) macrocyclic complex: structures, intermediates and reaction mechanism.

Authors:  Iryna A Koval; Catherine Belle; Katalin Selmeczi; Christian Philouze; Eric Saint-Aman; Anna Maria Schuitema; Patrick Gamez; Jean-Louis Pierre; Jan Reedijk
Journal:  J Biol Inorg Chem       Date:  2005-11-08       Impact factor: 3.358

2.  Validation of density functional modeling protocols on experimental bis(mu-oxo)/mu-eta2:eta2-peroxo dicopper equilibria.

Authors:  John L Lewin; David E Heppner; Christopher J Cramer
Journal:  J Biol Inorg Chem       Date:  2007-08-21       Impact factor: 3.358

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.