Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer

Chreifi, Georges; Baxter, Elizabeth L.; Doukov, Tzanko; Cohen, Aina E.; McPhillips, Scott E.; Song, Jinhu; Meharenna, Yergalem T.; Soltis, S. Michael; Poulos, Thomas L.

doi:10.1073/pnas.1521664113

Title: Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer

Journal Article · Tue Jan 19 00:00:00 EST 2016 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1521664113· OSTI ID:1236656

Chreifi, Georges ^[1]; Baxter, Elizabeth L. ^[2]; Doukov, Tzanko ^[2]; Cohen, Aina E. ^[2]; McPhillips, Scott E. ^[2]; Song, Jinhu ^[2]; Meharenna, Yergalem T. ^[1]; Soltis, S. Michael ^[2]; Poulos, Thomas L. ^[3]

Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900,
Macromolecular Crystallographic Group, The Stanford Synchrotron Radiation Lightsource, National Accelerator Laboratory, Stanford University, Stanford, CA 94309,
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900,, Department of Pharmaceutical Sciences, University of California, Irvine, CA 92697-3900,, Department of Chemistry, University of California, Irvine, CA 92697-3900

Significance A major problem in determining the crystal structures of metalloenzymes is that the reducing power of X-rays often changes the oxidation state of the metal center, thereby complicating important mechanistic conclusions on enzyme function. This reduction is especially problematic in studying Fe(IV)=O intermediates, which are powerful oxidants used by many metalloenzymes. This problem can be circumvented using the Stanford Linear Coherent Light Source (LCLS), which generates intense X-ray pulses on the femtosecond time scale and enables structure determinations with no reduction of metal centers. Here, we report the crystal structure of the Fe(IV)=O peroxidase intermediate called compound I using data obtained from the LCLS. We also present kinetic and computational results that, together with crystal structures, provide important mechanistic insights.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1236656

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Vol. 113 Journal Issue: 5; ISSN 0027-8424

Publisher:: Proceedings of the National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 53 works

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