title: Complex formation with the activator RACo affects the corrinoid structure of CoFeSP.
abstract: Activation of the corrinoid [Fe-S] protein (CoFeSP), involved in reductive CO(2) 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.
authors.affiliation: Technische Universität Berlin, Institut für Chemie, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany.
authors.forename: Wiebke
authors.initials: W
authors.lastname: Meister
authors.forename: Sandra E
authors.initials: SE
authors.lastname: Hennig
authors.forename: Jae-Hun
authors.initials: JH
authors.lastname: Jeoung
authors.forename: Friedhelm
authors.initials: F
authors.lastname: Lendzian
authors.forename: Holger
authors.initials: H
authors.lastname: Dobbek
authors.forename: Peter
authors.initials: P
authors.lastname: Hildebrandt
mesh_terms: D045728:Corrinoids / Q000737:chemistry* / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013059:Spectrum Analysis, Raman
chemical_list: D045728:Corrinoids; D007506:Iron-Sulfur Proteins