Structure of barley grain peroxidase refined at 1.9-Å resolution: a plant peroxidase reversibly inactivated at neutral pH
A Henriksen, KG Welinder, M Gajhede - Journal of Biological Chemistry, 1998 - ASBMB
The crystal structure of the major peroxidase of barley grain (BP 1) has been solved by
molecular replacement and phase combination and refined to an R-factor of 19.2% for all
data between 38 and 1.9 Å. The refined model includes amino acid residues 1–309, one
calcium ion, one sodium ion, iron-protoporphyrin IX, and 146 solvent molecules. BP 1 has
the apparently unique property of being unable to catalyze the reaction with the primary
substrate hydrogen peroxide to form compound I at pH values> 5, a feature investigated by …
molecular replacement and phase combination and refined to an R-factor of 19.2% for all
data between 38 and 1.9 Å. The refined model includes amino acid residues 1–309, one
calcium ion, one sodium ion, iron-protoporphyrin IX, and 146 solvent molecules. BP 1 has
the apparently unique property of being unable to catalyze the reaction with the primary
substrate hydrogen peroxide to form compound I at pH values> 5, a feature investigated by …
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