Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography.

@article{Henriksen1998StructuralIB,
  title={Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography.},
  author={Anette Henriksen and David Schuller and K{\aa}re Meno and Karen Gjesing Welinder and Andrew T. Smith and Michael Gajhede},
  journal={Biochemistry},
  year={1998},
  volume={37 22},
  pages={8054-60}
}
The three-dimensional structure of recombinant horseradish peroxidase in complex with BHA (benzhydroxamic acid) is the first structure of a peroxidase-substrate complex demonstrating the existence of an aromatic binding pocket. The crystal structure of the peroxidase-substrate complex has been determined to 2.0 A resolution with a crystallographic R-factor of 0.176 (R-free = 0. 192). A well-defined electron density for BHA is observed in the peroxidase active site, with a hydrophobic pocket… CONTINUE READING

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