The catalytic pathway of horseradish peroxidase at high resolution
By G. Berglund, G. Carlsson, Andrew T. Smith, H. Szöke, A. Henriksen, J. Hajdu. Nature, 2002
828 citations recorded by the source corpus.
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
Subfields: Inorganic Chemistry, Materials Chemistry, Structural Biology
View Paper: https://www.semanticscholar.org/paper/95e0815dffcde03532da545c5b4d7e04f1b2d474
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In Materials Chemistry
Citations in the corpus
- Horseradish peroxidase: a modern view of a classic enzyme. (2004, neutral): “High resolution crystal structures of the oxidised intermediates of HRP C confirm the importance of Arg38 and His42 for peroxide catalysis (Berglund et al., 2002).”
- Ultrahigh-throughput screening in drop-based microfluidics for directed evolution (2010, background): “Mutagenesis by epPCR will tend to bias mutations distant from the active site (24), and thus we create a second library using saturation mutagenesis to target specific residues at the entrance to the active site where the substrate binds (Protein Data Bank code 1HCH) (25).”