Complex of myoglobin with phenol bound in a proximal cavity

• 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

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.