The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata
Author:
Funder
Army Research Office
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference69 articles.
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3. An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata;Chen;J. Biol. Chem.,1996
4. The unusual reactivities of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazolate proximal heme iron ligand;Franzen;J. Am. Chem. Soc.,1998
5. Protein structure: an enzymatic globin from a marine worm;Lebioda;Nature,1999
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1. Structural Comparison of Substrate Binding Sites in Dehaloperoxidase A and B;Biochemistry;2024-07-03
2. Comparison of the Backbone Dynamics of Dehaloperoxidase-Hemoglobin Isoenzymes;The Journal of Physical Chemistry B;2024-04-02
3. Bridging the functional gap between reactivity and inhibition in dehaloperoxidase B from Amphitrite ornata: Mechanistic and structural studies with 2,4- and 2,6-dihalophenols;Journal of Inorganic Biochemistry;2022-11
4. Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature;IUCrJ;2022-07-25
5. Dehaloperoxidase: An enzymatic Swiss army knife;Coordination Chemistry Reviews;2021-08
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