Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase

被引:85
作者
Kovacs, Julie A. [1 ]
Brines, Lisa M. [1 ]
机构
[1] Univ Washington, Dept Chem, Seattle, WA 98195 USA
关键词
D O I
10.1021/ar600059h
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Toxic superoxide radicals, generated via adventitious reduction of dioxygen, have been implicated in a number of disease states. The cysteinate-ligated non-heme iron enzyme superoxide reductase (SOR) degrades superoxide via reduction. Biomimetic analogues which provide insight into why nature utilizes a trans-thiolate to promote SOR function are described. Spectroscopic and/or structural characterization of the first examples of thiolate-ligated Fe (III)peroxo complexes provides important benchmark parameters for the identification of biological intermediates. Oxidative addition of superoxide is favored by low redox potentials. The trans influence of the thiolate appears to significantly weaken the FeO peroxo bond, favoring proton-induced release of H2O2 from a high-spin Fe(III)OOH complex.
引用
收藏
页码:501 / 509
页数:9
相关论文
共 66 条
[1]   Roles of the proximal heme thiolate ligand in cytochrome P450cam [J].
Auclair, K ;
Moënne-Loccoz, P ;
de Montellano, PRO .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (21) :4877-4885
[2]   Effect of N-methylation of macrocyclic amine ligands on the spin state of iron(III):: A tale of two fluoro complexes [J].
Berry, JF ;
Bill, E ;
García-Serres, R ;
Neese, F ;
Weyhermüller, T ;
Wieghardt, K .
INORGANIC CHEMISTRY, 2006, 45 (05) :2027-2037
[3]   A thiolate-ligated nonheme oxoiron(IV) complex relevant to cytochrome P450 [J].
Bukowski, MR ;
Koehntop, KD ;
Stubna, A ;
Bominaar, EL ;
Halfen, JA ;
Münck, E ;
Nam, W ;
Que, L .
SCIENCE, 2005, 310 (5750) :1000-1002
[4]   Spin-state rationale for the peroxo-stabilizing role of the thiolate ligand in superoxide reductase [J].
Bukowski, MR ;
Halfen, HL ;
van den Berg, TA ;
Halfen, JA ;
Que, L .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (04) :584-587
[5]   Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase [J].
Clay, MD ;
Cosper, CA ;
Jenney, FE ;
Adams, MWW ;
Johnson, MK .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) :3796-3801
[6]   Spectroscopic studies of Pyrococcus furiosus superoxide reductase:: Implications for active-site structures and the catalytic mechanism [J].
Clay, MD ;
Jenney, FE ;
Hagedoorn, PL ;
George, GN ;
Adams, MWW ;
Johnson, MK .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (05) :788-805
[7]   ZINC, COBALT, AND CADMIUM THIOLATE COMPLEXES - MODELS FOR THE ZINC(S-CYS)2(HIS)2 CENTER IN TRANSCRIPTION FACTOR IIIA (CYS = CYSTEINE HIS = HISTIDINE) [J].
CORWIN, DT ;
GRUFF, ES ;
KOCH, SA .
JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS, 1987, (13) :966-967
[8]   Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates [J].
Costas, M ;
Mehn, MP ;
Jensen, MP ;
Que, L .
CHEMICAL REVIEWS, 2004, 104 (02) :939-986
[9]   Structure and chemistry of cytochrome P450 [J].
Denisov, IG ;
Makris, TM ;
Sligar, SG ;
Schlichting, I .
CHEMICAL REVIEWS, 2005, 105 (06) :2253-2277
[10]   Reactivity of five-coordinate models for the thiolate-ligated Fe site of nitrile hydratase [J].
Ellison, JJ ;
Nienstedt, A ;
Shoner, SC ;
Barnhart, D ;
Cowen, JA ;
Kovacs, JA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (23) :5691-5700