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  • Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.

Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.

Science (New York, N.Y.) (2014-07-12)
Cecilia M Casadei, Andrea Gumiero, Clive L Metcalfe, Emma J Murphy, Jaswir Basran, Maria Grazia Concilio, Susana C M Teixeira, Tobias E Schrader, Alistair J Fielding, Andreas Ostermann, Matthew P Blakeley, Emma L Raven, Peter C E Moody
摘要

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.

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