Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'
The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nan...
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2009
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 08329caa a22010697a 4500 | ||
|---|---|---|---|
| 001 | PAPER-8875 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203843.0 | ||
| 008 | 190411s2009 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-61649125434 | |
| 024 | 7 | |2 cas |a oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; superoxide, 11062-77-4; Archaeal Proteins; Oxidoreductases, 1.-; Superoxides, 11062-77-4; superoxide reductase, 1.- | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a PPCPF | ||
| 100 | 1 | |a Todorovic, S. | |
| 245 | 1 | 0 | |a Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant' |
| 260 | |c 2009 | ||
| 270 | 1 | 0 | |m Todorovic, S.; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da Republica 127, 2780-157 Oeiras, Portugal; email: smilja@itqb.unl.pt |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a ′natural variant′. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH. © 2009 the Owner Societies. |l eng | |
| 593 | |a Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da Republica 127, 2780-157 Oeiras, Portugal | ||
| 593 | |a Technische Universität Berlin, Institut für Festkörperphysik, Hardenbergstr. 26, D-10623 Berlin, Germany | ||
| 593 | |a Technische Universität Berlin, Institut für Chemie, Strasse des 17. Juni 135, D-10623 Berlin, Germany | ||
| 593 | |a Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pab. 2 piso 1, C1428EHA Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ARCHAEAL PROTEIN |
| 690 | 1 | 0 | |a OXIDOREDUCTASE |
| 690 | 1 | 0 | |a SUPEROXIDE |
| 690 | 1 | 0 | |a SUPEROXIDE REDUCTASE |
| 690 | 1 | 0 | |a ARCHAEOGLOBUS FULGIDUS |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CHEMISTRY |
| 690 | 1 | 0 | |a ENZYME ACTIVE SITE |
| 690 | 1 | 0 | |a ENZYMOLOGY |
| 690 | 1 | 0 | |a GENETICS |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a MUTATION |
| 690 | 1 | 0 | |a NANOARCHAEOTA |
| 690 | 1 | 0 | |a OXIDATION REDUCTION REACTION |
| 690 | 1 | 0 | |a RAMAN SPECTROMETRY |
| 690 | 1 | 0 | |a ARCHAEAL PROTEINS |
| 690 | 1 | 0 | |a ARCHAEOGLOBUS FULGIDUS |
| 690 | 1 | 0 | |a CATALYTIC DOMAIN |
| 690 | 1 | 0 | |a MUTATION |
| 690 | 1 | 0 | |a NANOARCHAEOTA |
| 690 | 1 | 0 | |a OXIDATION-REDUCTION |
| 690 | 1 | 0 | |a OXIDOREDUCTASES |
| 690 | 1 | 0 | |a SPECTRUM ANALYSIS, RAMAN |
| 690 | 1 | 0 | |a SUPEROXIDES |
| 700 | 1 | |a Rodrigues, J.V. | |
| 700 | 1 | |a Pinto, A.F. | |
| 700 | 1 | |a Thomsen, C. | |
| 700 | 1 | |a Hildebrandt, P. | |
| 700 | 1 | |a Teixeira, M. | |
| 700 | 1 | |a Murgida, D.H. | |
| 773 | 0 | |d 2009 |g v. 11 |h pp. 1809-1815 |k n. 11 |p Phys. Chem. Chem. Phys. |x 14639076 |t Physical Chemistry Chemical Physics | |
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| 856 | 4 | 0 | |u https://doi.org/10.1039/b815489a |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_14639076_v11_n11_p1809_Todorovic |y Handle |
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