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Journal Article

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

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

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Fulltext (public)

1944003.pdf
(Publisher version), 2MB

Supplementary Material (public)

1944003_Suppl_1.pdf
(Supplementary material), 126KB

1944003_Suppl_2.pdf
(Supplementary material), 21KB

1944003_Suppl_3.pdf
(Supplementary material), 20KB

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: http://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.