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Rubredoxin as a paramagnetic relaxation-inducing probe
- Source :
-
Journal of Inorganic Biochemistry . Sep2009, Vol. 103 Issue 9, p1245-1253. 9p. - Publication Year :
- 2009
-
Abstract
- Abstract: The paramagnetic effect due to the presence of a metal center with unpaired electrons is no longer considered a hindrance in protein NMR spectroscopy. In the present work, the paramagnetic effect due to the presence of a metal center with unpaired electrons was used to map the interface of an electron transfer complex. Desulfovibrio gigas cytochrome c 3 was chosen as target to study the effect of the paramagnetic probe, Fe-rubredoxin, which produced specific line broadening in the heme IV methyl resonances M21 and M181. The rubredoxin binding surface in the complex with cytochrome c 3 was identified in a heteronuclear 2D NMR titration. The identified heme methyls on cytochrome c 3 are involved in the binding interface of the complex, a result that is in agreement with the predicted complexes obtained by restrained molecular docking, which shows a cluster of possible solutions near heme IV. The use of a paramagnetic probe in 1HNMR titration and the mapping of the complex interface, in combination with a molecular simulation algorithm proved to be a valuable strategy to study electron transfer complexes involving non-heme iron proteins and cytochromes. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 01620134
- Volume :
- 103
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Journal of Inorganic Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 44008949
- Full Text :
- https://doi.org/10.1016/j.jinorgbio.2009.07.006