4cvi

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Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperatureNeutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperature

Structural highlights

4cvi is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Hybrid , Neutron Diffraction , X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Publication Abstract from PubMed

Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O-O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.

Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.,Casadei CM, Gumiero A, Metcalfe CL, Murphy EJ, Basran J, Concilio MG, Teixeira SC, Schrader TE, Fielding AJ, Ostermann A, Blakeley MP, Raven EL, Moody PC Science. 2014 Jul 11;345(6193):193-7. doi: 10.1126/science.1254398. Epub 2014 Jul, 10. PMID:25013070[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Casadei CM, Gumiero A, Metcalfe CL, Murphy EJ, Basran J, Concilio MG, Teixeira SC, Schrader TE, Fielding AJ, Ostermann A, Blakeley MP, Raven EL, Moody PC. Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase. Science. 2014 Jul 11;345(6193):193-7. doi: 10.1126/science.1254398. Epub 2014 Jul, 10. PMID:25013070 doi:http://dx.doi.org/10.1126/science.1254398

4cvi, resolution 2.10Å

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