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Peptide methionine sulfoxide reductase A (MsrA): direct electrochemical oxidation on carbon electrodes.
Bioelectrochemistry. 2013 Feb; 89:11-8.B

Abstract

The direct electrochemical behaviour of peptide methionine sulfoxide reductase A (MsrA) adsorbed on glassy carbon and boron doped diamond electrodes surface, was studied over a wide pH range by cyclic and differential pulse voltammetry. MsrA oxidation mechanism occurs in three consecutive, pH dependent steps, corresponding to the oxidation of tyrosine, tryptophan and histidine amino acid residues. At the glassy carbon electrode, the first step corresponds to the oxidation of tyrosine and tryptophan residues and occurs for the same potential. The advantage of boron doped diamond electrode was to enable the separation of tyrosine and tryptophan oxidation peaks. On the second step occurs the histidine oxidation, and on the third, at higher potentials, the second tryptophan oxidation. MsrA adsorbs on the hydrophobic carbon electrode surface preferentially through the three hydrophobic domains, C1, C2 and C3, which contain the tyrosine, tryptophan and histidine residues, and tryptophan exists only in these regions, and undergo electrochemical oxidation.

Authors+Show Affiliations

Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade de Coimbra, 3004-535 Coimbra, Portugal.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22967951

Citation

Enache, T A., and A M. Oliveira-Brett. "Peptide Methionine Sulfoxide Reductase a (MsrA): Direct Electrochemical Oxidation On Carbon Electrodes." Bioelectrochemistry (Amsterdam, Netherlands), vol. 89, 2013, pp. 11-8.
Enache TA, Oliveira-Brett AM. Peptide methionine sulfoxide reductase A (MsrA): direct electrochemical oxidation on carbon electrodes. Bioelectrochemistry. 2013;89:11-8.
Enache, T. A., & Oliveira-Brett, A. M. (2013). Peptide methionine sulfoxide reductase A (MsrA): direct electrochemical oxidation on carbon electrodes. Bioelectrochemistry (Amsterdam, Netherlands), 89, 11-8. https://doi.org/10.1016/j.bioelechem.2012.08.004
Enache TA, Oliveira-Brett AM. Peptide Methionine Sulfoxide Reductase a (MsrA): Direct Electrochemical Oxidation On Carbon Electrodes. Bioelectrochemistry. 2013;89:11-8. PubMed PMID: 22967951.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Peptide methionine sulfoxide reductase A (MsrA): direct electrochemical oxidation on carbon electrodes. AU - Enache,T A, AU - Oliveira-Brett,A M, Y1 - 2012/08/21/ PY - 2012/06/22/received PY - 2012/08/07/revised PY - 2012/08/08/accepted PY - 2012/9/13/entrez PY - 2012/9/13/pubmed PY - 2013/6/12/medline SP - 11 EP - 8 JF - Bioelectrochemistry (Amsterdam, Netherlands) JO - Bioelectrochemistry VL - 89 N2 - The direct electrochemical behaviour of peptide methionine sulfoxide reductase A (MsrA) adsorbed on glassy carbon and boron doped diamond electrodes surface, was studied over a wide pH range by cyclic and differential pulse voltammetry. MsrA oxidation mechanism occurs in three consecutive, pH dependent steps, corresponding to the oxidation of tyrosine, tryptophan and histidine amino acid residues. At the glassy carbon electrode, the first step corresponds to the oxidation of tyrosine and tryptophan residues and occurs for the same potential. The advantage of boron doped diamond electrode was to enable the separation of tyrosine and tryptophan oxidation peaks. On the second step occurs the histidine oxidation, and on the third, at higher potentials, the second tryptophan oxidation. MsrA adsorbs on the hydrophobic carbon electrode surface preferentially through the three hydrophobic domains, C1, C2 and C3, which contain the tyrosine, tryptophan and histidine residues, and tryptophan exists only in these regions, and undergo electrochemical oxidation. SN - 1878-562X UR - https://www.unboundmedicine.com/medline/citation/22967951/Peptide_methionine_sulfoxide_reductase_A__MsrA_:_direct_electrochemical_oxidation_on_carbon_electrodes_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1567-5394(12)00126-0 DB - PRIME DP - Unbound Medicine ER -