4CVI

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

Summary for 4CVI

• Entry DOI: 10.2210/pdb4cvi/pdb
• Related: 4CVJ
• Descriptor: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxidoreductase, heme peroxidase, redox, electron transport, ferric, heme, neutron
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 34245.89

Authors

Casadei, C.M.,Gumiero, A.,Blakeley, M.P.,Ostermann, A.,Raven, E.L.,Moody, P.C.E. (deposition date: 2014-03-27, release date: 2014-07-16, Last modification date: 2024-05-08)

Primary citation

Casadei, C.M.,Gumiero, A.,Metcalfe, C.L.,Murphy, E.J.,Basran, J.,Concilio, M.G.,Teixeira, S.C.M.,Schrader, T.E.,Fielding, A.J.,Ostermann, A.,Blakeley, M.P.,Raven, E.L.,Moody, P.C.E.
Neutron Cryo-Crystallography Captures the Protonation State of Ferryl Heme in a Peroxidase
Science, 345:193-, 2014

PubMed Abstract: 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.

PubMed: 25013070
DOI: 10.1126/SCIENCE.1254398

Experimental method

NEUTRON DIFFRACTION (2.407 Å)
X-RAY DIFFRACTION (2.1 Å)