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  • Title: Iron ligand recognition by monomeric hemoglobins.
    Author: Stephanos JJ, Farina SA, Addison AW.
    Journal: Biochim Biophys Acta; 1996 Jul 18; 1295(2):209-21. PubMed ID: 8695648.
    Abstract:
    Binding affinities of monomeric Glycera dibranchiata hemoglobin for some anions and heterocyclic amines, including imidazoles, pyrazole, triazole and tetrazole have been evaluated and compared with those of sperm whale and horse heart myoglobin. The proteins' affinities for substituted heterocyclic amines are strongly influenced by the steric bulk and flexibility of the aromatic ring. The ligand coordination mode depends on the heme oxidation state, iron(III) amine adducts being more stable than the iron(II) adducts, the higher affinities of stronger Brønsted-Lowry bases reflecting their essentially sigma-donor character. The bifunctional molecule morpholinoethylisocyanide acts as a redox-state-dependent ambidentate ligand, binding as an N-donor to iron(III), but as a C-donor to iron(II). pH-Dependences of the ESR and optical spectra of the azole adducts reveal iron-linked ionisations and spin-equilibria in the heme pocket. Enthalpy and entropy changes for the binding process were estimated for several ligands, and mutually compensatory behaviour is observed globally for delta H degree and delta S degree. At the compensation temperature theta, the binding affinities of monomeric Glycera dibranchiata hemoglobin and sperm whale myoglobin are similar and associated with free energy changes delta G degree (theta) approximately -9 +/- 1 kJ mol-1 for the heterocyclic and anionic ligands.
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