The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata

The activation of dehaloperoxidase-hemoglobin (DHP) to form a ferryl intermediate requires the distal histidine, H55, to act as an acid base catalyst. The lack of ancillary amino acids in the distal pocket to assist in this process makes H55 even more important to the formation of active intermediat...

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Veröffentlicht in:Biochimica et biophysica acta 2013-10, Vol.1834 (10), p.2020-2029
Hauptverfasser: Jiang, Shu, Wright, Iain, Swartz, Paul, Franzen, Stefan
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Sprache:eng
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