5JQR
The Structure of Ascorbate Peroxidase Compound II formed by reaction with m-CPBA
Summary for 5JQR
| Entry DOI | 10.2210/pdb5jqr/pdb |
| Related | 2XIF 5JPR |
| Descriptor | Ascorbate peroxidase, PROTOPORPHYRIN IX CONTAINING FE, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | heme peroxidase, intermediates, compound ii, ferryl, multicrystal, oxidoreductase |
| Biological source | Glycine max (Soybean) |
| Total number of polymer chains | 1 |
| Total formula weight | 27804.08 |
| Authors | Kwon, H.,Raven, E.L.,Moody, P.C.E. (deposition date: 2016-05-05, release date: 2016-12-21, Last modification date: 2024-01-10) |
| Primary citation | Kwon, H.,Basran, J.,Casadei, C.M.,Fielding, A.J.,Schrader, T.E.,Ostermann, A.,Devos, J.M.,Aller, P.,Blakeley, M.P.,Moody, P.C.,Raven, E.L. Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme. Nat Commun, 7:13445-13445, 2016 Cited by PubMed Abstract: Catalytic heme enzymes carry out a wide range of oxidations in biology. They have in common a mechanism that requires formation of highly oxidized ferryl intermediates. It is these ferryl intermediates that provide the catalytic engine to drive the biological activity. Unravelling the nature of the ferryl species is of fundamental and widespread importance. The essential question is whether the ferryl is best described as a Fe(IV)=O or a Fe(IV)-OH species, but previous spectroscopic and X-ray crystallographic studies have not been able to unambiguously differentiate between the two species. Here we use a different approach. We report a neutron crystal structure of the ferryl intermediate in Compound II of a heme peroxidase; the structure allows the protonation states of the ferryl heme to be directly observed. This, together with pre-steady state kinetic analyses, electron paramagnetic resonance spectroscopy and single crystal X-ray fluorescence, identifies a Fe(IV)-OH species as the reactive intermediate. The structure establishes a precedent for the formation of Fe(IV)-OH in a peroxidase. PubMed: 27897163DOI: 10.1038/ncomms13445 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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