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Sci. Lett. J. 2013, 2: 33
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Research Article
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Full Text
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Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin
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Sabarinathan K. Gopalasubramaniama,e, Kalyan C. Kondapallib,f, César Millán-Pachecoc, Nina Pastorc, Timothy L. Stemmlerb, Jose F. Morand, Raúl Arredondo-Petera
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a Lab. de Biofísica y Biología Molecular, Universidad Autónoma del Estado de Morelos, Ave. Universidad 1001, Col. Chamilpa, 62210 Cuernavaca, Morelos, México
b Dept. of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, Detroit, Michigan 48201, USA
c Fac. de Ciencias, Universidad Autónoma del Estado de Morelos, Ave. Universidad 1001, Col. Chamilpa, 62210 Cuernavaca, Morelos, México
d Depto. de Ciencias del Medio Natural/Dept. of Environmental Sciences, Public University of Navarre, Spain
e Present address: Dept. of Soil Science and Agricultural Chemistry, Tamil Nadu Agricultural University, Tamil Nadu, India
f Present address: School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA
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Abstract |
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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+.
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Keywords
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Fluorescence quenching; Hemoglobin; Isothermal calorimetry; Non-symbiotic; Oryza sativa; Protein-protein interaction
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