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To establish conditions to study the oligomeric assembly of heme-binding protein (HbpS) in solution by applying the tools of site-directed spin labeling combined with pulse electron paramagnetic resonance (SDSL EPR) spectroscopy, as well as to analyze redox stress-based conformational changes in HbpS subunits within the oligomer in solution. In vivo elucidation of molecular mechanisms that control the downregulation of the novel redox-system HbpS-SenS-SenR.

antioxidants and redox signaling

Conformational Changes in the Novel Redox Sensor Protein HbpS Studied by Site-Directed Spin Labeling and Its Turnover in Dependence on the Catalase-Peroxidase CpeB