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Complex Formation with the Activator RACo Affects the Corrinoid Structure of CoFeSP
Citation key Meister2012
Author Meister, Wiebke and Hennig, Sandra E. and Jeoung, Jae-Hun and Lendzian, Friedhelm and Dobbek, Holger and Hildebrandt, Peter
Pages 7040–7042
Year 2012
DOI 10.1021/bi300795n
Journal Biochemistry
Volume 51
Number 36
Month sep
Abstract Activation of the corrinoid [Fe-S] protein (CoFeSP), involved in reductive CO2 conversion, requires the reduction of the Co(II) center by the [Fe-S] protein RACo, which according to the reduction potentials of the two proteins would correspond to an uphill electron transfer. In our resonance Raman spectroscopic work, we demonstrate that, as a conformational gate for the corrinoid reduction, complex formation of Co(II)FeSP and RACo specifically alters the structure of the corrinoid cofactor by modifying the interactions of the Co(II) center with the axial ligand. On the basis of various deletion mutants, the potential interaction domains on the partner proteins can be predicted.
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