Reduction of dioxygen by enzymes containing copper
- 20 May 2006
- journal article
- review article
- Published by Springer Nature in JBIC Journal of Biological Inorganic Chemistry
- Vol. 11 (5) , 539-547
- https://doi.org/10.1007/s00775-006-0114-9
Abstract
The reduction of dioxygen is a key step in many important biological processes including respiration and ligand oxidation. Enzymes containing either iron or copper or, indeed, both elements are often involved in this process, yet the catalytic mechanisms employed are not fully understood at the current time despite intensive biochemical, spectroscopic and structural studies. The aim of this article is to highlight the current structural knowledge regarding the process of dioxygen reduction using examples of copper-containing enzymes.Keywords
This publication has 54 references indexed in Scilit:
- Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complexJBIC Journal of Biological Inorganic Chemistry, 2004
- Oxidant types in copper–dioxygen chemistry: the ligand coordination defines the Cu n -O2 structure and subsequent reactivityJBIC Journal of Biological Inorganic Chemistry, 2004
- The Protein Data BankNucleic Acids Research, 2000
- Crystal structure of a plant catechol oxidase containing a dicopper centerNature Structural & Molecular Biology, 1998
- Cytochrome oxidase: pathways for electron tunneling and proton transferJBIC Journal of Biological Inorganic Chemistry, 1998
- Multicopper Oxidases and OxygenasesChemical Reviews, 1996
- Crystal Structure of a Free Radical Enzyme, Galactose OxidaseJournal of Molecular Biology, 1994
- X-ray Structures and Mechanistic Implications of Three Functional Derivatives of Ascorbate Oxidase from ZucchiniJournal of Molecular Biology, 1993
- Refined crystal structure of ascorbate oxidase at 1.9 Å resolutionJournal of Molecular Biology, 1992
- X-ray crystal structure of the blue oxidase ascorbate oxidase from ZucchiniJournal of Molecular Biology, 1989