Hemoglobin and related heme proteins, generally referred to as ‘globins’, reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexacoordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.
Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family / D. de Sanctis, A. Pesce, M. Nardini, M. Bolognesi, A. Bocedi, P. Ascenzi. - In: IUBMB LIFE. - ISSN 1521-6543. - 56:11-12(2004), pp. 643-651.
Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
M. Nardini;M. Bolognesi;
2004
Abstract
Hemoglobin and related heme proteins, generally referred to as ‘globins’, reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexacoordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.Pubblicazioni consigliate
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