Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1
Fecha
2013Autor
Versión
Acceso abierto / Sarbide irekia
Tipo
Artículo / Artikulua
Versión
Versión aceptada / Onetsi den bertsioa
Impacto
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nodoi-noplumx
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Resumen
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 i ...
[++]
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+. [--]
Materias
Fluorescence quenching,
Hemoglobin,
Isothermal calorimetry,
Non-symbiotic,
Oryza sativa,
Protein-protein interaction
Editor
Simplex Academic Publishers
Publicado en
ScienceJet 2013, 2: 33
Departamento
Universidad Pública de Navarra. Departamento de Ciencias del Medio Natural /
Nafarroako Unibertsitate Publikoa. Natura Ingurunearen Zientziak Saila
Entidades Financiadoras
This work was funded by CoNaCyT (project no. 42873Q), México (to R. A.-P.), Dept. of Education, Government of Navarre (no. 999–2006), Spain (to J. F. M.) and NIDDKD (DK068139), USA (to T. L. S.).