Article · Wikipedia archive · Last revised Jul 30, 2026

Neuroglobin

Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated protostomes, like photosynthetic acoel as well as radiata such as jellyfish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain and in the physiological seal brain. This is thought to be due to convergent evolution. It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research confirmed the presence of human neuroglobin protein in cerebrospinal fluid (CSF).

Last revised
Jul 30, 2026
Read time
≈ 3 min
Length
726 w
Citations
17
Source
Wikipedia ↗
NGB
Identifiers
AliasesNGB, neuroglobin
External IDsOMIM: 605304; MGI: 2151886; HomoloGene: 10942; GeneCards: NGB; OMA:NGB - orthologs
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
SpeciesHumanMouse
Entrez

58157

64242

Ensembl

ENSG00000165553

ENSMUSG00000021032

UniProt

Q9NPG2

Q9ER97

RefSeq (mRNA)

NM_021257

NM_001294308
NM_022414

RefSeq (protein)

NP_067080

NP_001281237
NP_071859

Location (UCSC)Chr 14: 77.27 – 77.27 MbChr 12: 87.14 – 87.15 Mb
PubMed search34
Wikidata
View/Edit HumanView/Edit Mouse
Neuroglobin
Model of murine neuroglobin from PDB: 1Q1F​
Identifiers
SymbolNGB
NCBI gene58157
HGNC6553
OMIM605304
UniProtQ9NPG2
Other data
LocusChr. 14 q24
Search for
StructuresSwiss-model
DomainsInterPro

Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated protostomes, like photosynthetic acoel as well as radiata such as jellyfish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain56 and in the physiological seal brain.7 This is thought to be due to convergent evolution.8 It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research confirmed the presence of human neuroglobin protein in cerebrospinal fluid (CSF).9

Neuroglobin was first identified by Thorsten Burmester et al. in 2000.10

The 3D structure of human neuroglobin was determined in 2003.11 The next year, murine neuroglobin was determined at a higher resolution.12

A practical treatment for carbon monoxide poisoning based on binding of CO by neuroglobin (Ngb) with a mutated distal histidine (H64Q) appears to be possible.13

See also

See also

References

References

  1. GRCh38: Ensembl release 89: ENSG00000165553 – Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000021032 – Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. DellaValle B, Hempel C, Kurtzhals JA, Penkowa M (August 2010). "In vivo expression of neuroglobin in reactive astrocytes during neuropathology in murine models of traumatic brain injury, cerebral malaria, and autoimmune encephalitis". Glia. 58 (10): 1220–7. doi:10.1002/glia.21002. PMID 20544857. S2CID 8563830.
  6. De Marinis E, Acaz-Fonseca E, Arevalo MA, et al. (March 2013). "17β-Oestradiol anti-inflammatory effects in primary astrocytes require oestrogen receptor β-mediated neuroglobin up-regulation" (PDF). Journal of Neuroendocrinology. 25 (3): 260–70. doi:10.1111/jne.12007. PMID 23190172. S2CID 12425782.
  7. Mitz SA, Reuss S, Folkow LP, et al. (October 2009). "When the brain goes diving: glial oxidative metabolism may confer hypoxia tolerance to the seal brain". Neuroscience. 163 (2): 552–60. doi:10.1016/j.neuroscience.2009.06.058. PMID 19576963. S2CID 207246404.
  8. science.gov, Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity by Lechauve, Christophe; Jager, Muriel; Laguerre, Laurent; Kiger, Laurent; Correc, Gaelle; Leroux, Cedric; Vinogradov, Serge; Czjzek, Mirjam; Marden, Michael C.; Bail
  9. Casado B, Pannell LK, Whalen G, Clauw DJ, Baraniuk JN (February 2005). "Human neuroglobin protein in cerebrospinal fluid" (PDF). Proteome Science. 3 (1): 2. doi:10.1186/1477-5956-3-2. PMC 554085. PMID 15730566.
  10. Burmester T, Weich B, Reinhardt S, Hankeln T (September 2000). "A vertebrate globin expressed in the brain". Nature. 407 (6803): 520–3. Bibcode:2000Natur.407..520B. doi:10.1038/35035093. PMID 11029004. S2CID 4337897.
  11. Alessandra Pesce; Sylvia Dewilde; Marco Nardini; Luc Moens; Paolo Ascenzi; Thomas Hankeln; Thorsten Burmester & Martino Bolognes (2003). "Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity". Structure. 11 (9): 1087–1095. doi:10.1016/S0969-2126(03)00166-7. hdl:10067/455310151162165141. PMID 12962627.
  12. Beatrice Vallone; Karin Nienhaus; Maurizio Brunori; G. Ulrich Nienhaus (2004). "The structure of murine neuroglobin: Novel pathways for ligand migration and binding". Proteins: Structure, Function, and Bioinformatics. 56 (1): 85–92. doi:10.1002/prot.20113. PMID 15162488. S2CID 29990150.
  13. Rydzewski, J; Nowak, W (2018). "Photoinduced transport in an H64Q neuroglobin antidote for carbon monoxide poisoning". The Journal of Chemical Physics. 148 (11): 115101. Bibcode:2018JChPh.148k5101R. doi:10.1063/1.5013659. PMID 29566507.
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