Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin

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

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Neuroglobin (Ngb) and cytoglobin (Cygb) are two recently discovered intracellular members of the vertebrate hemoglobin (Hb) family. Ngb, predominantly expressed in nerve cells, is of ancient evolutionary origin and is homologous to nerve-globins of invertebrates. Cygb, present in many different tissues, shares common ancestry with myoglobin (Mb) and can be traced to early vertebrate evolution. Ngb is held to facilitate O2 diffusion to the mitochondria and to protect neuronal cells from hypoxic-ischemic insults, may be an oxidative stress-responsive sensor protein for signal transduction, and may carry out enzymatic activities, such as NO/O2 scavenging. Cygb is linked to collagen synthesis, may provide O2 for enzymatic reactions, and may be involved in a ROS (NO)-signaling pathway(s). Ngb and Cgb display the classical three-over-three α-helical fold of Hb and Mb, and are endowed with a hexa-coordinate heme-Fe atom, in their ferrous and ferric forms, having the heme distal HisE7 residue as the endogenous ligand. Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of Ngb and Cygb. Moreover, Ngb and Cygb display a tunnel/cavity system within the protein matrix held to facilitate ligand channeling to/from the heme, multiple ligand copies storage, multi-ligand reactions, and conformational transitions supporting ligand binding.

Original languageEnglish
Pages (from-to)657-664
Number of pages8
JournalIUBMB Life
Volume56
Issue number11-12
DOIs
Publication statusPublished - Nov 2004

Fingerprint

Rubiaceae
Heme
Ligands
Atoms
Myoglobin
Vertebrates
Hemoglobins
Signal transduction
Mitochondria
Oxidative stress
Globins
Scavenging
Invertebrates
Neurons
neuroglobin
cytoglobin
Signal Transduction
Tunnels
Proteins
Oxidative Stress

Keywords

  • Cytoglobin
  • Hemoglobin
  • Myoglobin
  • Neuroglobin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., ... Bolognesi, M. (2004). Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. IUBMB Life, 56(11-12), 657-664. https://doi.org/10.1080/15216540500078830

Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. / Pesce, Alessandra; De Sanctis, Daniele; Nardini, Marco; Dewilde, Sylvia; Moens, Luc; Hankeln, Thomas; Burmester, Thorsten; Ascenzi, Paolo; Bolognesi, Martino.

In: IUBMB Life, Vol. 56, No. 11-12, 11.2004, p. 657-664.

Research output: Contribution to journalArticle

Pesce, A, De Sanctis, D, Nardini, M, Dewilde, S, Moens, L, Hankeln, T, Burmester, T, Ascenzi, P & Bolognesi, M 2004, 'Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin', IUBMB Life, vol. 56, no. 11-12, pp. 657-664. https://doi.org/10.1080/15216540500078830
Pesce, Alessandra ; De Sanctis, Daniele ; Nardini, Marco ; Dewilde, Sylvia ; Moens, Luc ; Hankeln, Thomas ; Burmester, Thorsten ; Ascenzi, Paolo ; Bolognesi, Martino. / Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. In: IUBMB Life. 2004 ; Vol. 56, No. 11-12. pp. 657-664.
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