Complex of myoglobin with phenol bound in a proximal cavity

The structure of a complex of sperm whale myoglobin with phenol places this inhibitor of the haloperoxidase activity in a proximal cavity that is unlikely to be the halophenol binding site. The absence of phenol binding at the heme edge, where dehalogenation is likely to take place, indicates that t...

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Bibliographic Details
Published in:Acta Crystallographica Section F Structural Biology and Crystallization Communications
Main Authors: Huang, Xiao, Wang, Chunxue, Celeste, Lesa R., Lovelace, Leslie L., Sun, Shenfang, Dawson, John H., Lebioda, Lukasz
Format: Text
Language:English
Published: International Union of Crystallography 2012
Subjects:
Structural Communications
Sperm whale
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509966
http://www.ncbi.nlm.nih.gov/pubmed/23192025
https://doi.org/10.1107/S1744309112045514
Description
Summary:The structure of a complex of sperm whale myoglobin with phenol places this inhibitor of the haloperoxidase activity in a proximal cavity that is unlikely to be the halophenol binding site. The absence of phenol binding at the heme edge, where dehalogenation is likely to take place, indicates that the inhibitor and the halophenol substrates only bind in the active site in the presence of hydrogen peroxide.

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