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

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.

journal_name

Arch Biochem Biophys

authors

D'Angelo P,Zitolo A,Pacello F,Mancini G,Proux O,Hazemann JL,Desideri A,Battistoni A

doi

10.1016/j.abb.2010.03.010

subject

Has Abstract

pub_date

2010-06-01 00:00:00

pages

43-9

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(10)00095-0

journal_volume

498

pub_type

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