Abstract
Hemoglobin and related heme proteins, generally referred to as 'globins', reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexa-coordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.
| Original language | English |
|---|---|
| Pages (from-to) | 643-651 |
| Number of pages | 9 |
| Journal | IUBMB Life |
| Volume | 56 |
| Issue number | 11-12 |
| DOIs | |
| Publication status | Published - Nov 2004 |
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Keywords
- Cytoglobin
- Hemoglobin
- Hexacoordinate heme
- Myoglobin
- Neuroglobin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family. / De Sanctis, Daniele; Pesce, Alessandra; Nardini, Marco; Bolognesi, Martino; Bocedi, Alessio; Ascenzi, Paolo.
In: IUBMB Life, Vol. 56, No. 11-12, 11.2004, p. 643-651.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
AU - De Sanctis, Daniele
AU - Pesce, Alessandra
AU - Nardini, Marco
AU - Bolognesi, Martino
AU - Bocedi, Alessio
AU - Ascenzi, Paolo
PY - 2004/11
Y1 - 2004/11
N2 - Hemoglobin and related heme proteins, generally referred to as 'globins', reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexa-coordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.
AB - Hemoglobin and related heme proteins, generally referred to as 'globins', reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexa-coordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.
KW - Cytoglobin
KW - Hemoglobin
KW - Hexacoordinate heme
KW - Myoglobin
KW - Neuroglobin
UR - http://www.scopus.com/inward/record.url?scp=17144408393&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=17144408393&partnerID=8YFLogxK
U2 - 10.1080/15216540500059640
DO - 10.1080/15216540500059640
M3 - Article
C2 - 15844231
AN - SCOPUS:17144408393
VL - 56
SP - 643
EP - 651
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 11-12
ER -