The human brain hexacoordinated neuroglobin three-dimensional structure

Alessandra Pesce, Sylvia Dewilde, Marco Nardini, Luc Moens, Paolo Ascenzi, Thomas Hankeln, Thorsten Burmester, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review


Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O2 supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a six-coordinated heme. O2 and CO bind to the heme-iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold, adapted to host the reversible bis-histidyl heme complex, and an elongated protein matrix cavity, held to facilitate O2 diffusion to the heme. The structure of neuroglobin suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

Original languageEnglish
Pages (from-to)63-65
Number of pages3
Issue number1-2
Publication statusPublished - Jan 2004


  • Globin fold
  • Heme hexacoordination
  • Neuroglobin
  • Oxygen affinity
  • Protein cavities

ASJC Scopus subject areas

  • Cell Biology
  • Materials Science(all)
  • Instrumentation


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