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Literature summary for 1.13.11.49 extracted from

  • De Schutter, A.; Correia, H.D.; Freire, D.M.; Rivas, M.G.; Rizzi, A.; Santos-Silva, T.; Gonzalez, P.J.; Van Doorslaer, S.
    Ligand binding to chlorite dismutase from Magnetospirillum sp (2015), J. Phys. Chem. B, 119, 13859-13869 .
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with thiocyanate and azide, to 0.976 and 1.0 A resolution, respectively. The crystal structure of the Cld-azide complex reveals a single well-defined orientation of the azide molecule in the heme pocket. EPR shows a pH-dependent heme structure, probably due to acid-base transitions of the surrounding amino-acid residues stabilizing azide Magnetospirillum sp.

Organism

Organism UniProt Comment Textmining
Magnetospirillum sp. A0A0M3KL46
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Cofactor

Cofactor Comment Organism Structure
heme wild-type Cld shows a variety of low- and high-spin ferric heme forms. Addition of an axial ligand, such as azide or imidazole, removes this heterogeneity almost entirely Magnetospirillum sp.