Reductive elimination of superoxide: structure and mechanism of superoxide reductases

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Superoxide anion is among the deleterious reactive oxygen species, towards which all organisms have specialized detoxifying enzymes. For quite a long time, superoxide elimination was thought to occur through its dismutation, catalyzed by Fe, Cu, and Mn or, as more recently discovered, by Ni-containing enzymes. However, during the last decade, a novel type of enzyme was established that eliminates superoxide through its reduction: the superoxide reductases, which are spread among anaerobic and facultative microorganisms, from the three life kingdoms. These enzymes share the same unique catalytic site, an iron ion bound to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant of similar to 10(9) M-1 s(-1). In this review, the properties of these enzymes will be thoroughly discussed.
Original languageUnknown
Pages (from-to)285-297
JournalBiochimica Et Biophysica Acta-Proteins And Proteomics
Volume1804
Issue number2
DOIs
Publication statusPublished - 1 Jan 2010

Cite this

@article{ebe9e30204cb4d88bd82299c101d6392,
title = "Reductive elimination of superoxide: structure and mechanism of superoxide reductases",
abstract = "Superoxide anion is among the deleterious reactive oxygen species, towards which all organisms have specialized detoxifying enzymes. For quite a long time, superoxide elimination was thought to occur through its dismutation, catalyzed by Fe, Cu, and Mn or, as more recently discovered, by Ni-containing enzymes. However, during the last decade, a novel type of enzyme was established that eliminates superoxide through its reduction: the superoxide reductases, which are spread among anaerobic and facultative microorganisms, from the three life kingdoms. These enzymes share the same unique catalytic site, an iron ion bound to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant of similar to 10(9) M-1 s(-1). In this review, the properties of these enzymes will be thoroughly discussed.",
keywords = "ARCHAEOGLOBUS-FULGIDUS, ESCHERICHIA-COLI, RUBREDOXIN OXIDOREDUCTASE, RBO GENE-PRODUCT, DESULFOVIBRIO-VULGARIS HILDENBOROUGH, OXYGEN DETOXIFICATION, DESULFOARCULUS-BAARSII, ACTIVE-SITE, NONHEME IRON PROTEIN, TREPONEMA-PALLIDUM",
author = "Teixeira, {Miguel Nuno}",
note = "Pinto, Ana Filipa Rodrigues, Joao V. (ITQB)",
year = "2010",
month = "1",
day = "1",
doi = "10.1016/j.bbapap.2009.10.011",
language = "Unknown",
volume = "1804",
pages = "285--297",
journal = "Biochimica Et Biophysica Acta-Proteins And Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Reductive elimination of superoxide: structure and mechanism of superoxide reductases

AU - Teixeira, Miguel Nuno

N1 - Pinto, Ana Filipa Rodrigues, Joao V. (ITQB)

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Superoxide anion is among the deleterious reactive oxygen species, towards which all organisms have specialized detoxifying enzymes. For quite a long time, superoxide elimination was thought to occur through its dismutation, catalyzed by Fe, Cu, and Mn or, as more recently discovered, by Ni-containing enzymes. However, during the last decade, a novel type of enzyme was established that eliminates superoxide through its reduction: the superoxide reductases, which are spread among anaerobic and facultative microorganisms, from the three life kingdoms. These enzymes share the same unique catalytic site, an iron ion bound to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant of similar to 10(9) M-1 s(-1). In this review, the properties of these enzymes will be thoroughly discussed.

AB - Superoxide anion is among the deleterious reactive oxygen species, towards which all organisms have specialized detoxifying enzymes. For quite a long time, superoxide elimination was thought to occur through its dismutation, catalyzed by Fe, Cu, and Mn or, as more recently discovered, by Ni-containing enzymes. However, during the last decade, a novel type of enzyme was established that eliminates superoxide through its reduction: the superoxide reductases, which are spread among anaerobic and facultative microorganisms, from the three life kingdoms. These enzymes share the same unique catalytic site, an iron ion bound to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant of similar to 10(9) M-1 s(-1). In this review, the properties of these enzymes will be thoroughly discussed.

KW - ARCHAEOGLOBUS-FULGIDUS

KW - ESCHERICHIA-COLI

KW - RUBREDOXIN OXIDOREDUCTASE

KW - RBO GENE-PRODUCT

KW - DESULFOVIBRIO-VULGARIS HILDENBOROUGH

KW - OXYGEN DETOXIFICATION

KW - DESULFOARCULUS-BAARSII

KW - ACTIVE-SITE

KW - NONHEME IRON PROTEIN

KW - TREPONEMA-PALLIDUM

U2 - 10.1016/j.bbapap.2009.10.011

DO - 10.1016/j.bbapap.2009.10.011

M3 - Article

VL - 1804

SP - 285

EP - 297

JO - Biochimica Et Biophysica Acta-Proteins And Proteomics

JF - Biochimica Et Biophysica Acta-Proteins And Proteomics

SN - 1570-9639

IS - 2

ER -