Literature DB >> 11377434

Pulse radiolysis studies on superoxide reductase from Treponema pallidum.

V Nivière1, M Lombard, M Fontecave, C Houée-Levin.   

Abstract

Superoxide reductases (SORs) are small metalloenzymes, which catalyze reduction of O2*- to H2O2. The reaction of the enzyme from Treponema pallidum with superoxide was studied by pulse radiolysis methods. The first step is an extremely fast bi-molecular reaction of the ferrous center with O2, with a rate constant of 6 x 10 (8) M(-1) s(-1). A first intermediate is formed which is converted to a second one with a slower rate constant of 4800 s(-1). This latter value is 10 times higher than the corresponding one previously reported in the case of SOR from Desulfoarculus baarsii. The reconstituted spectra for the two intermediates are consistent with formation of transient iron-peroxide species.

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Year:  2001        PMID: 11377434     DOI: 10.1016/s0014-5793(01)02468-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  16 in total

Review 1.  Discovery of superoxide reductase: an historical perspective.

Authors:  Vincent Nivière; Marc Fontecave
Journal:  J Biol Inorg Chem       Date:  2004-01-13       Impact factor: 3.358

Review 2.  Synthetic analogues of cysteinate-ligated non-heme iron and non-corrinoid cobalt enzymes.

Authors:  Julie A Kovacs
Journal:  Chem Rev       Date:  2004-02       Impact factor: 60.622

Review 3.  Superoxide dismutases and superoxide reductases.

Authors:  Yuewei Sheng; Isabel A Abreu; Diane E Cabelli; Michael J Maroney; Anne-Frances Miller; Miguel Teixeira; Joan Selverstone Valentine
Journal:  Chem Rev       Date:  2014-04-01       Impact factor: 60.622

4.  Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxin.

Authors:  João V Rodrigues; Lígia M Saraiva; Isabel A Abreu; Miguel Teixeira; Diane E Cabelli
Journal:  J Biol Inorg Chem       Date:  2006-10-26       Impact factor: 3.358

5.  X-ray absorption spectroscopy and reactivity of thiolate-ligated Fe(III)-OOR complexes.

Authors:  Jay Stasser; Frances Namuswe; Gary D Kasper; Yunbo Jiang; Courtney M Krest; Michael T Green; James Penner-Hahn; David P Goldberg
Journal:  Inorg Chem       Date:  2010-10-18       Impact factor: 5.165

6.  Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxin.

Authors:  Françoise Auchère; Robert Sikkink; Cristina Cordas; Patricia Raleiras; Pedro Tavares; Isabel Moura; José J G Moura
Journal:  J Biol Inorg Chem       Date:  2004-08-20       Impact factor: 3.358

7.  Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases.

Authors:  Françoise Auchère; Sofia R Pauleta; Pedro Tavares; Isabel Moura; José J G Moura
Journal:  J Biol Inorg Chem       Date:  2006-03-17       Impact factor: 3.358

8.  Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand.

Authors:  João V Rodrigues; Bruno L Victor; Harald Huber; Lígia M Saraiva; Cláudio M Soares; Diane E Cabelli; Miguel Teixeira
Journal:  J Biol Inorg Chem       Date:  2007-10-30       Impact factor: 3.358

9.  Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivity.

Authors:  Abhishek Dey; Francis E Jenney; Michael W W Adams; Michael K Johnson; Keith O Hodgson; Britt Hedman; Edward I Solomon
Journal:  J Am Chem Soc       Date:  2007-09-22       Impact factor: 15.419

10.  Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris.

Authors:  Michael D Clay; Joseph P Emerson; Eric D Coulter; Donald M Kurtz; Michael K Johnson
Journal:  J Biol Inorg Chem       Date:  2003-05-23       Impact factor: 3.358

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