Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity

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

Research output: Contribution to journalArticlepeer-review

Abstract

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 hexacoordinated 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 neuroglobin structure 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)1087-1095
Number of pages9
JournalStructure
Volume11
Issue number9
DOIs
Publication statusPublished - Sep 1 2003

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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