1HCH

Structure of horseradish peroxidase C1A compound I

Summary for 1HCH

• Entry DOI: 10.2210/pdb1hch/pdb
• Related: 1ATJ 2ATJ 3ATJ 6ATJ 7ATJ
• Descriptor: PEROXIDASE C1A, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, peroxidase, horseradish, catalytic intermediate, compound i
• Biological source: ARMORACIA RUSTICANA (HORSERADISH)
• Cellular location: Secreted (Probable): P00433
• Total number of polymer chains: 1
• Total formula weight: 34518.65

Authors

Berglund, G.I.,Carlsson, G.H.,Hajdu, J.,Smith, A.T.,Szoke, H.,Henriksen, A. (deposition date: 2001-05-04, release date: 2002-07-19, Last modification date: 2011-07-13)

Primary citation

Berglund, G.I.,Carlsson, G.H.,Smith, A.T.,Szoke, H.,Henriksen, A.,Hajdu, J.
The Catalytic Pathway of Horseradish Peroxidase at High Resolution
Nature, 417:463-, 2002

PubMed Abstract: 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.

PubMed: 12024218
DOI: 10.1038/417463A

Experimental method

X-RAY DIFFRACTION (1.57 Å)