Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin
Articolo
Data di Pubblicazione:
2004
Citazione:
Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin / A. Pesce, D. De Sanctis, M. Nardini, S. Dewilde, L. Moens, T. Hankeln, T. Burmester, P. Ascenzi, M. Bolognesi. - In: IUBMB LIFE. - ISSN 1521-6543. - 56:11-12(2004), pp. 657-664. [10.1080/15216540500078830]
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 threeover-
three a-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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Cytoglobin; Hemoglobin; Myoglobin; Neuroglobin
Elenco autori:
A. Pesce, D. De Sanctis, M. Nardini, S. Dewilde, L. Moens, T. Hankeln, T. Burmester, P. Ascenzi, M. Bolognesi
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