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 language | English |
|---|---|
| Pages (from-to) | 657-664 |
| Number of pages | 8 |
| Journal | IUBMB Life |
| Volume | 56 |
| Issue number | 11-12 |
| DOIs | |
| Publication status | Published - Nov 2004 |
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Keywords
- Cytoglobin
- Hemoglobin
- Myoglobin
- Neuroglobin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
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 journal › Article
}
TY - JOUR
T1 - Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin
AU - Pesce, Alessandra
AU - De Sanctis, Daniele
AU - Nardini, Marco
AU - Dewilde, Sylvia
AU - Moens, Luc
AU - Hankeln, Thomas
AU - Burmester, Thorsten
AU - Ascenzi, Paolo
AU - Bolognesi, Martino
PY - 2004/11
Y1 - 2004/11
N2 - 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.
AB - 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.
KW - Cytoglobin
KW - Hemoglobin
KW - Myoglobin
KW - Neuroglobin
UR - http://www.scopus.com/inward/record.url?scp=17144382480&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=17144382480&partnerID=8YFLogxK
U2 - 10.1080/15216540500078830
DO - 10.1080/15216540500078830
M3 - Article
C2 - 15804829
AN - SCOPUS:17144382480
VL - 56
SP - 657
EP - 664
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 11-12
ER -