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

Daniele De Sanctis, Alessandra Pesce, Marco Nardini, Martino Bolognesi, Alessio Bocedi, Paolo Ascenzi

Research output: Contribution to journalArticlepeer-review


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 languageEnglish
Pages (from-to)643-651
Number of pages9
JournalIUBMB Life
Issue number11-12
Publication statusPublished - Nov 2004


  • Cytoglobin
  • Hemoglobin
  • Hexacoordinate heme
  • Myoglobin
  • Neuroglobin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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