Gopalasubramaniama, Sabarinathan K.Kondapallib, Kalyan C.Millán-Pacheco, CésarPastor, NinaStemmler, Timothy L.Morán Juez, José FernandoArredondo-Peter, Raúl2019-06-072019-06-072013https://academica-e.unavarra.es/handle/2454/33266Ferrous oxygenated hemoglobins (Hb2+O2) autoxidize to ferric Hb3+, but Hb3+ is reduced to Hb2+ by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb13+). Spectroscopic analysis showed that FLbR2 reduces Hb13+. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb13+, however the use of ITC and IEF techniques revealed that this interaction is weak. In silico modeling showed that predicted FLbR2 and native Hb13+ interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb13+.13 p.application/pdfengFluorescence quenchingHemoglobinIsothermal calorimetryNon-symbioticOryza sativaProtein-protein interactioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccess