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Unraveling structural features of flavodiiron proteins: a detailed structural insight for oxygen or nitric oxide reduction
Publication . Borges, Patrícia Alexandra Teixeira; Romão, Célia V.; Frazão, Carlos
"The work presented in this dissertation focuses on Flavodiiron Proteins (FDPs), a family of enzymes able to reduce oxygen and/or nitric oxide into water or non-toxic nitrous oxide. FDPs are widespread in prokaryotes and unicellular eukaryotes as well as in phototrophs, from cyanobacteria and unicellular algae to higher plants. The FDP minimal structural unit is composed of two domains: a metallo-β-lactamase- like domain at the N-terminal harbouring a diiron catalytic center and a flavodoxin-like domain at the C-terminal containing a non-covalently bound flavin mononucleotide (FMN). The diiron site is where the substrate reduction occurs while the FMN cofactor shuttles the electrons to this catalytic center. The two redox centers within the same monomer are too far away (~40 Å) to allow an efficient electron transfer between them. Therefore, the minimal functional unit of FDPs, consists of a homodimer with a “head-to-tail” arrangement, which brings close together (~6 Å) the diiron center of one monomer and the FMN cofactor of the neighbouring monomer. (...)"
Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
Publication . Soares, Jéssica; Teixeira, Miguel
"Flavodiiron proteins (FDPs) are a family of metalloproteins involved in the reduction of molecular oxygen and hydrogen peroxide to water and/or the reduction of nitric oxide to nitrous oxide.
Bioinformatic analysis of the primary structure of the FDPs led to the identification of a conserved motif in class B FDPs (flavorubredoxins, FlRd), that is relatively close to the active centre. The present experimental work aimed to study the role played by two serines present in this motif in an FDP from E.coli. Thus, two mutants, S33D and S34D, were studied and characterized in order to determine the implications of such mutations on the biochemical, kinetic and spectroscopic properties of the enzyme. The production of the mutants was achieved in E. coli BL21 (DE3) Gold and it was found that the biochemical characteristics were kept almost unchanged.(...)"
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Fundação para a Ciência e a Tecnologia
Programa de financiamento
3599-PPCDT
Número da atribuição
PTDC/BBB-BQB/3135/2014