Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme

Hanna Kwon, Jaswir Basran, Cecilia M. Casadei, Alistair J. Fielding, Tobias E. Schrader, Andreas Ostermann, Juliette M. Devos, Pierre Aller, Matthew P. Blakeley, Peter C. E. Moody () and Emma L. Raven ()
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Hanna Kwon: University of Leicester
Jaswir Basran: University of Leicester
Cecilia M. Casadei: University of Leicester
Alistair J. Fielding: The Photon Science Institute and School of Chemistry, The University of Manchester
Tobias E. Schrader: Jülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH
Andreas Ostermann: Heinz Maier-Leibnitz Zentrum (MLZ), Technische Universität München
Juliette M. Devos: Institut Laue-Langevin
Pierre Aller: Diamond Light Source Ltd, Diamond House, Harwell Science and Innovation Campus
Matthew P. Blakeley: Institut Laue-Langevin
Peter C. E. Moody: University of Leicester
Emma L. Raven: University of Leicester

Nature Communications, 2016, vol. 7, issue 1, 1-6

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13445

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