Peroxidase activation of cytoglobin by anionic phospholipids: Mechanisms and consequences

摘要: Cytoglobin (Cygb) is a hexa-coordinated hemoprotein with yet to be defined physiological functions. The iron coordination and spin state of the Cygb heme group are sensitive oxidation two cysteine residues (Cys38/Cys83) and/or binding free fatty acids. However, roles redox vs lipid regulators Cygb's structural rearrangements in context protein peroxidase competence not known. Searching for physiologically relevant Cygb, here we report that anionic phospholipids, particularly phosphatidylinositolphosphates, affect organization modulate its activity both conjointly independently oxidation. Thus, different lipids can operate cysteine-dependent cysteine-independent ways as inducers activity. We establish utilized catalysis peroxidation phospholipids (including phosphatidylinositolphosphates) yielding mono-oxygenated molecular species. Combined computational simulations propose bipartite model rationalizes modes interactions effects on re-arrangements hemoprotein.