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1H5L

X-ray induced reduction of horseradish peroxidase C1A Compound III (89-100% dose)

Summary for 1H5L
Entry DOI10.2210/pdb1h5l/pdb
Related1ATJ 1GW2 1GWO 1GWT 1GWU 1GX2 1H55 1H57 1H58 1H5A 1H5C 1H5D 1H5E 1H5F 1H5G 1H5H 1H5I 1H5J 1H5K 1H5M 1HCH 2ATJ 3ATJ 6ATJ 7ATJ
DescriptorPEROXIDASE C1A, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (6 entities in total)
Functional Keywordsoxidoreductase, peroxidase, horseradish, compound iii, oxyperoxidase, x-ray induced reduction
Biological sourceARMORACIA RUSTICANA (HORSERADISH)
Cellular locationSecreted (Probable): P00433
Total number of polymer chains1
Total formula weight34771.86
Authors
Berglund, G.I.,Carlsson, G.H.,Hajdu, J.,Smith, A.T.,Szoke, H.,Henriksen, A. (deposition date: 2001-05-22, release date: 2002-06-21, Last modification date: 2011-07-13)
Primary citationBerglund, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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