Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin(287 views) Mazzarella L, Merlino A, Vitagliano L, Verde C, Di Prisco G, Peisach J, Vergara A
Keywords: Cyanidation, Haemoglobins, Structural Modifications, Tetrameric, X Ray Crystal Structures,
Affiliations: *** IBB - CNR ***
Dept of Chemical Sciences, University of Naples Federico II, Naples, Italy
Institute of Biostructures and Bioimaging, CNR, Naples, Italy
Institute of Biosciences and BioResources, CNR, Naples, Italy
Roma 3 University, Dept of Biology, Rome, Italy
Dept of Biophysics and Physiology, Albert Einstein College of Medicine, New York NY, United States
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Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin
Ferric cold-adapted fish haemoglobins exhibit heterogeneous coordination at the alpha (aquo-met) and beta (bis-histidyl) subunits. Herein we report two EPR-distinct bis-histidyl conformers (I and II) of the beta subunits of ferric haemoglobin from Trematomus bernacchii which react differently with CN-. An EPR titration reveals that upon cyanidation the most distorted conformer I reacts faster than II, producing both a cyanided and penta-coordinate ferric forms in the b subunits. The X-ray crystal structure of the partially cyanided conformer I reveals both an order-disorder transition and details of a communication between alpha and beta subunits.
Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin
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Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin