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

被引：3

作者：

D'Angelo, Paola ^{[1
]}

Zitolo, Andrea ^{[1
]}

Pacello, Francesca ^{[2
]}

Mancini, Giordano ^{[3
]}

Proux, Olivier ^{[4
]}

Hazemann, Jean Louis ^{[5
]}

Desideri, Alessandro ^{[2
]}

Battistoni, Andrea ^{[2
]}

机构：

[1] Univ Roma La Sapienza, Dept Chem, I-00185 Rome, Italy

[2] Univ Roma Tor Vergata, Dept Biol, I-00133 Rome, Italy

[3] Consortium Supercomp Applicat, CASPUR, I-00185 Rome, Italy

[4] Univ Grenoble 1, UMS CNRS, Observ Sci Univers Grenoble, F-38041 Grenoble, France

[5] CNRS, UPR2940, Inst Neel, F-38042 Grenoble 9, France

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2010年 / 498卷 / 01期

关键词：

Hemeproteins; EXAFS; XANES; Superoxide dismutase; Synchrotron radiation; PHOTOLYZED CARBONMONOXY-MYOGLOBIN; MULTIPLE-SCATTERING PROCEDURE; BODY DISTRIBUTION-FUNCTIONS; CONDENSED MATTER; MOLECULAR STEREOCHEMISTRY; CRYSTAL-STRUCTURES; FINE-STRUCTURE; N-TERMINUS; LIGAND; COMPLEXES;

D O I：

10.1016/j.abb.2010.03.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 0.02 angstrom 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-home 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. (c) 2010 Elsevier Inc. All rights reserved.

引用

页码：43 / 49

页数：7

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