Structure and quantum chemical characterization of chloroperoxidase compound 0, 
a common reaction intermediate of diverse heme enzymes.

Kühnel, K.; Derat, E.; Derner, J.; Shaik, S.; Schlichting, I.

doi:10.1073/pnas.0606285103

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Journal Article

Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes.

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Kühnel, K.
Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society;

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1944003_Suppl_2.pdf
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1944003_Suppl_3.pdf
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Citation

Kühnel, K., Derat, E., Derner, J., Shaik, S., & Schlichting, I. (2007). Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes. Proceedings of the National Academy of Sciences of the United States of America, 104(1), 99-104. doi:10.1073/pnas.0606285103.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-8AFF-8

Abstract

We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-Å resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long OGraphicO bond length of 1.5 Å and a FeGraphicO bond distance of 1.8 Å, which is also observed in the crystal structure.