Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 105

1.

Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide.

Molina-Heredia FP, Houée-Levin C, Berthomieu C, Touati D, Tremey E, Favaudon V, Adam V, Nivière V.

Proc Natl Acad Sci U S A. 2006 Oct 3;103(40):14750-5.

2.

Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.

Adam V, Royant A, Nivière V, Molina-Heredia FP, Bourgeois D.

Structure. 2004 Sep;12(9):1729-40.

3.

Photochemical processes observed during the reaction of superoxide reductase from Desulfoarculus baarsii with superoxide: re-evaluation of the reaction mechanism.

Bonnot F, Houée-Levin C, Favaudon V, Nivière V.

Biochim Biophys Acta. 2010 Apr;1804(4):762-7. doi: 10.1016/j.bbapap.2009.11.019.

PMID:
19962458
4.

Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism.

Clay MD, Jenney FE Jr, Hagedoorn PL, George GN, Adams MW, Johnson MK.

J Am Chem Soc. 2002 Feb 6;124(5):788-805.

PMID:
11817955
5.

Superoxide reductase from Desulfoarculus baarsii: identification of protonation steps in the enzymatic mechanism.

Nivière V, Asso M, Weill CO, Lombard M, Guigliarelli B, Favaudon V, Houée-Levin C.

Biochemistry. 2004 Jan 27;43(3):808-18.

PMID:
14730986
6.

Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii.

Mathé C, Mattioli TA, Horner O, Lombard M, Latour JM, Fontecave M, Nivière V.

J Am Chem Soc. 2002 May 8;124(18):4966-7.

PMID:
11982354
7.

Control of the evolution of iron peroxide intermediate in superoxide reductase from Desulfoarculus baarsii. Involvement of lysine 48 in protonation.

Bonnot F, Molle T, Ménage S, Moreau Y, Duval S, Favaudon V, Houée-Levin C, Nivière V.

J Am Chem Soc. 2012 Mar 21;134(11):5120-30. doi: 10.1021/ja209297n.

PMID:
22360372
8.

Mössbauer characterization of an unusual high-spin side-on peroxo-Fe3+ species in the active site of superoxide reductase from Desulfoarculus Baarsii. Density functional calculations on related models.

Horner O, Mouesca JM, Oddou JL, Jeandey C, Nivière V, Mattioli TA, Mathé C, Fontecave M, Maldivi P, Bonville P, Halfen JA, Latour JM.

Biochemistry. 2004 Jul 13;43(27):8815-25.

PMID:
15236590
9.

Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii.

Mathé C, Weill CO, Mattioli TA, Berthomieu C, Houée-Levin C, Tremey E, Nivière V.

J Biol Chem. 2007 Jul 27;282(30):22207-16.

10.

The superoxide reductase from the early diverging eukaryote Giardia intestinalis.

Testa F, Mastronicola D, Cabelli DE, Bordi E, Pucillo LP, Sarti P, Saraiva LM, Giuffrè A, Teixeira M.

Free Radic Biol Med. 2011 Oct 15;51(8):1567-74. doi: 10.1016/j.freeradbiomed.2011.07.017.

PMID:
21839165
11.

Kinetics of the superoxide reductase catalytic cycle.

Emerson JP, Coulter ED, Phillips RS, Kurtz DM Jr.

J Biol Chem. 2003 Oct 10;278(41):39662-8.

12.

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

Clay MD, Emerson JP, Coulter ED, Kurtz DM Jr, Johnson MK.

J Biol Inorg Chem. 2003 Jul;8(6):671-82.

PMID:
12764688
14.

Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii.

Mathé C, Nivière V, Houée-Levin C, Mattioli TA.

Biophys Chem. 2006 Jan 1;119(1):38-48.

PMID:
16084640
15.

Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin.

Kurtz DM Jr.

J Inorg Biochem. 2006 Apr;100(4):679-93. Review.

PMID:
16504301
16.

Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis.

Lombard M, Houée-Levin C, Touati D, Fontecave M, Nivière V.

Biochemistry. 2001 Apr 24;40(16):5032-40.

PMID:
11305919
17.

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.

Katona G, Carpentier P, Nivière V, Amara P, Adam V, Ohana J, Tsanov N, Bourgeois D.

Science. 2007 Apr 20;316(5823):449-53.

18.

Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxin.

Rodrigues JV, Saraiva LM, Abreu IA, Teixeira M, Cabelli DE.

J Biol Inorg Chem. 2007 Feb;12(2):248-56.

PMID:
17066300
19.

Enhanced superoxide and hydrogen peroxide detection in biological assays.

Rodrigues JV, Gomes CM.

Free Radic Biol Med. 2010 Jul 1;49(1):61-6. doi: 10.1016/j.freeradbiomed.2010.03.014.

PMID:
20332022
20.

Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris.

Emerson JP, Coulter ED, Cabelli DE, Phillips RS, Kurtz DM Jr.

Biochemistry. 2002 Apr 2;41(13):4348-57.

PMID:
11914081

Supplemental Content

Support Center