| Literature DB >> 25431759 |
Sabarinathan K Gopalasubramaniam1, Kalyan C Kondapalli2, César Millán-Pacheco3, Nina Pastor3, Timothy L Stemmler2, Jose F Moran4, Raúl Arredondo-Peter1.
Abstract
Ferrous 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+.Entities:
Keywords: Fluorescence quenching; Hemoglobin; Isothermal calorimetry; Non-symbiotic; Oryza sativa; Protein-protein interaction
Year: 2013 PMID: 25431759 PMCID: PMC4243682
Source DB: PubMed Journal: Scijet ISSN: 2278-3393