Carbon monoxide binding to the heme group at the dimeric interface modulates structure and copper accessibility in the Cu,Zn superoxide dismutase fromHaemophilus ducreyi: in silico andin vitroevidences-Reference-Cited by-同舟云学术

Carbon monoxide binding to the heme group at the dimeric interface modulates structure and copper accessibility in the Cu,Zn superoxide dismutase fromHaemophilus ducreyi: in silico andin vitroevidences

Published:2012-07 Issue:3 Volume:30 Page:269-279
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Chillemi Giovanni,De Santis Serena,Falconi Mattia,Mancini Giordano,Migliorati Valentina,Battistoni Andrea,Pacello Francesca,Desideri Alessandro,D’Angelo Paola

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883

Reference39 articles.

1. A Histidine-rich Metal Binding Domain at the N Terminus of Cu,Zn-Superoxide Dismutases from Pathogenic Bacteria

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3. Geometrical fitting of experimental XANES spectra by a full multiple-scattering procedure

4. Interaction Models for Water in Relation to Protein Hydration

5. GROMACS: A message-passing parallel molecular dynamics implementation

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