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 hexa-coordinate 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.
Original language | English |
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Pages (from-to) | 643-651 |
Number of pages | 9 |
Journal | IUBMB Life |
Volume | 56 |
Issue number | 11-12 |
DOIs | |
Publication status | Published - Nov 2004 |
Keywords
- Cytoglobin
- Hemoglobin
- Hexacoordinate heme
- Myoglobin
- Neuroglobin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology