Goncalves 2013 Abstract IOC75

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Goncalves V (2013) FLAVODIIRON PROTEINS: A Novel Type of Oxygen/Nitric Oxide Reductases. Mitochondr Physiol Network 18.03.

Link: IOC75 Open Access

Goncalves V, Pinto L, Testa F, Giuffre A, Sarti P, Vicente JB, Teixeira M (2013)

Event: IOC75

Flavodiiron proteins (FDPs) are a family of oxygen and/or nitric oxide reductase enzymes, found in prokaryotic as well as in eukaryotic sources. This family of enzymes has a common core formed by a metallo-β-lactamase-like and flavodoxin domains. These domains harbor, respectively, a diiron catalytic center and a flavin mononucleotide. Despite the structural and functional data on FDPs, the molecular determinants that define their substrate specificity remain to be clarified. Therefore, two FDPs with known and opposite substrate selectivity were chosen to be studied: the nitric oxide reducing-FDP from Escherichia coli and an oxygen-reducing-FDP from Entamoeba histolytica, a pathogenic protozoan. The amino acid sequences and 3D structural data were compared, and single and double site specific mutants were generated based on differences found near the catalytic center. The kinetic and thermodynamic properties of these mutants were analyzed by stopped-flow absorption and electron paramagnetic resonance spectroscopies, potentiometric-coupled spectroscopic studies and oxygen/nitric oxide amperometry. The activities of the FDPs having oxygen and nitric oxide as substrates were determined. Furthermore, it was also evaluated whether these proteins produced reactive oxygen species.

Keywords: FLAVOIIRON Proteins, Oxygen Reductases, Nitric Oxide Reductases

O2k-Network Lab: IT Roma Sarti P, PT Oieras Teixeira M


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Affiliations and author contributions

Gonçalves, V. L. 1,2; Pinto, L.1; Testa, F. 3,4; Giuffrè, A.3,4; Sarti, P.3,4; Vicente, J. B.2; Teixeira, M.1

  1. Metalloenzymes and Molecular Bioenergetics Group, ITQB, New University of Lisbon, Oeiras, Portugal
  2. Metabolism and Genetics Group, iMed.UL, Faculty of Pharmacy, University of Lisbon, Portugal
  3. Department of Biochemical Sciences, Sapienza University of Rome, Italy
  4. CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, Italy


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