Unraveling the Redox Properties of the Global Regulator FurA from Anabaena sp. PCC 7120: Disulfide Reductase Activity Based on Its CXXC Motifs
作者： Laura Botello-Morte , M. Teresa Bes , Begoña Heras , Ángela Fernández-Otal , M. Luisa Peleato
关键词: Plasma protein binding 、 Cofactor 、 Redox 、 Anabaena 、 Enzyme activator 、 Biochemistry 、 DNA 、 Biology 、 Cysteine 、 Regulator
摘要: Abstract Cyanobacterial FurA works as a global regulator linking iron homeostasis to photosynthetic metabolism and the responses different environmental stresses. Additionally, modulates several genes involved in redox fulfills characteristics of heme-sensor protein whose interaction with this cofactor negatively affects its DNA binding ability. from Anabaena PCC 7120 contains five cysteine residues, four them arranged two CXXC motifs. Aims: Our goals were analyze depth putative contribution these motifs properties identify potential interacting partners regulator. Results: Insulin reduction assays unravel that exhibits disulfide reductase activity. Simultaneous presence both signatures greatly enhances rate, although motif containing Cys101 Cys104 seems major contributor Disulfide activity was not detected other ferric uptake regula...
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