We have carried out an X-ray Absorption Spectroscopy (XAS) study of ferric, ferrous, CO- and NO-bound Haemophilus ducreyi Cu,ZnSOD (HdSOD) in solution to investigate the structural modifications induced by the binding of small gaseous ligands to heme in this enzyme. The combined analysis of EXAFS and XANES data has allowed us to characterize the local structure around the Fe-heme with 0.02A accuracy, revealing a heterogeneity in the distances between iron and the two histidine ligands which was not evident in the X-ray crystal structure. In addition, we have shown that the metal oxidation state does not influence the Fe-heme coordination environment, whereas the presence of the CO and NO ligands induces local structural rearrangements in the enzyme which are very similar to those already observed in other hexa-coordinated heme proteins, such as neuroglobin.

D'Angelo, P., Zitolo, A., Pacello, F., Mancini, G., Proux, O., Hazemann, J., et al. (2010). Fe-heme structure in Cu, Zn superoxide dismutase from Haemophilus ducreyi by X-ray absorption spectroscopy. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 498(1), 43-49 [10.1016/j.abb.2010.03.010].

Fe-heme structure in Cu, Zn superoxide dismutase from Haemophilus ducreyi by X-ray absorption spectroscopy

PACELLO, FRANCESCA;DESIDERI, ALESSANDRO;BATTISTONI, ANDREA
2010-06-01

Abstract

We have carried out an X-ray Absorption Spectroscopy (XAS) study of ferric, ferrous, CO- and NO-bound Haemophilus ducreyi Cu,ZnSOD (HdSOD) in solution to investigate the structural modifications induced by the binding of small gaseous ligands to heme in this enzyme. The combined analysis of EXAFS and XANES data has allowed us to characterize the local structure around the Fe-heme with 0.02A accuracy, revealing a heterogeneity in the distances between iron and the two histidine ligands which was not evident in the X-ray crystal structure. In addition, we have shown that the metal oxidation state does not influence the Fe-heme coordination environment, whereas the presence of the CO and NO ligands induces local structural rearrangements in the enzyme which are very similar to those already observed in other hexa-coordinated heme proteins, such as neuroglobin.
1-giu-2010
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Ferrous Compounds; Protein Conformation; Haemophilus ducreyi; Copper; Iron; Zinc; Models, Molecular; Nitric Oxide; X-Ray Absorption Spectroscopy; Carbon Monoxide; Ferric Compounds; Heme; Ligands; Superoxide Dismutase
http://www.sciencedirect.com/science/article/pii/S0003986110000950
D'Angelo, P., Zitolo, A., Pacello, F., Mancini, G., Proux, O., Hazemann, J., et al. (2010). Fe-heme structure in Cu, Zn superoxide dismutase from Haemophilus ducreyi by X-ray absorption spectroscopy. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 498(1), 43-49 [10.1016/j.abb.2010.03.010].
D'Angelo, P; Zitolo, A; Pacello, F; Mancini, G; Proux, O; Hazemann, J; Desideri, A; Battistoni, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/10625
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