Hemoglobin and related heme proteins reversibly bind gaseus diatomic ligands (O2, NO, CO) to a penta-coordinate heme Fe atom, the ligand filling the sixth coordination site. Several new globins have recently been reported to display a functionally-relevant hexacoordinate (6C) heme Fe atom, whose sixth coordination site is filled by an endogenous His protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates O2, NO, CO ligand binding properties of 6C-globins. Here, we present the results of three-year investigations carried over in our lab on the crystal structures of 6C-hemoglobins from human brain, human tissues, and from Drosophila. Mechanisms for 6C-5C transitions are discussed on structural grounds.

Structure-function relationships in the growing hexa-coordinate globin sub-family / A. Pesce, D. de Sanctis, M. Nardini, M. Bolognesi - In: MMD-meeting workbook: Poster Session / CNR-INFM. - [s.l] : CNR-INFM, 2005. - pp. 267-267 (( convegno MMD Meeting, Matter, Materials and Devices tenutosi a Genova nel 2005.

Structure-function relationships in the growing hexa-coordinate globin sub-family

M. Nardini;M. Bolognesi
2005

Abstract

Hemoglobin and related heme proteins reversibly bind gaseus diatomic ligands (O2, NO, CO) to a penta-coordinate heme Fe atom, the ligand filling the sixth coordination site. Several new globins have recently been reported to display a functionally-relevant hexacoordinate (6C) heme Fe atom, whose sixth coordination site is filled by an endogenous His protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates O2, NO, CO ligand binding properties of 6C-globins. Here, we present the results of three-year investigations carried over in our lab on the crystal structures of 6C-hemoglobins from human brain, human tissues, and from Drosophila. Mechanisms for 6C-5C transitions are discussed on structural grounds.
Settore BIO/10 - Biochimica
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/8864
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