Review abstract
Nature Chemical Biology 4, 186 - 193 (2008)
Published online: 15 February 2008 | doi:10.1038/nchembio.71
Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
Elena G Kovaleva1 & John D Lipscomb1
Abstract
Oxidase and oxygenase enzymes allow the use of relatively unreactive O2 in biochemical reactions. Many of the mechanistic strategies used in nature for this key reaction are represented within the 2-histidine-1-carboxylate facial triad family of non-heme Fe(II)-containing enzymes. The open face of the metal coordination sphere opposite the three endogenous ligands participates directly in the reaction chemistry. Here, data from several studies are presented showing that reductive O2 activation within this family is initiated by substrate (and in some cases cosubstrate or cofactor) binding, which then allows coordination of O2 to the metal. From this starting point, the O2 activation process and the reactions with substrates diverge broadly. The reactive species formed in these reactions have been proposed to encompass four oxidation states of iron and all forms of reduced O2 as well as several of the reactive oxygen species that derive from O-O bond cleavage.
- Department of Biochemistry, Molecular Biology and Biophysics and the Center for Metals in Biocatalysis, University of Minnesota, 6-155 Jackson Hall, Minneapolis, Minnesota 55455, USA.
Correspondence to: Elena G Kovaleva1 e-mail: koval021@umn.edu
Correspondence to: John D Lipscomb1 e-mail: lipsc001@umn.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
One motif ? many different reactionsNature Structural Biology News and Views (01 Mar 2000)
The most versatile of all reactive intermediates?Nature Chemical Biology News and Views (01 Feb 2007)
See all 3 matches for News And ViewsRESEARCH
The structural basis of cephalosporin formation in a mononuclear ferrous enzymeNature Structural & Molecular Biology Article (01 Jan 2004)
See all 12 matches for Research