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

Abstract

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.

Authors:
 [1];  [2];  [2];  [2];  [2];  [2];  [1];  [2];  [3]
  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900,
  2. Macromolecular Crystallographic Group, The Stanford Synchrotron Radiation Lightsource, National Accelerator Laboratory, Stanford University, Stanford, CA 94309,
  3. 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
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1236656
Grant/Contract Number:  
AC02-76SF00515
Resource Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Volume: 113 Journal Issue: 5; Journal ID: ISSN 0027-8424
Publisher:
Proceedings of the National Academy of Sciences
Country of Publication:
United States
Language:
English

Citation Formats

Chreifi, Georges, Baxter, Elizabeth L., Doukov, Tzanko, Cohen, Aina E., McPhillips, Scott E., Song, Jinhu, Meharenna, Yergalem T., Soltis, S. Michael, and Poulos, Thomas L. Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer. United States: N. p., 2016. Web. doi:10.1073/pnas.1521664113.
Chreifi, Georges, Baxter, Elizabeth L., Doukov, Tzanko, Cohen, Aina E., McPhillips, Scott E., Song, Jinhu, Meharenna, Yergalem T., Soltis, S. Michael, & Poulos, Thomas L. Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer. United States. https://doi.org/10.1073/pnas.1521664113
Chreifi, Georges, Baxter, Elizabeth L., Doukov, Tzanko, Cohen, Aina E., McPhillips, Scott E., Song, Jinhu, Meharenna, Yergalem T., Soltis, S. Michael, and Poulos, Thomas L. Tue . "Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer". United States. https://doi.org/10.1073/pnas.1521664113.
@article{osti_1236656,
title = {Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer},
author = {Chreifi, Georges and Baxter, Elizabeth L. and Doukov, Tzanko and Cohen, Aina E. and McPhillips, Scott E. and Song, Jinhu and Meharenna, Yergalem T. and Soltis, S. Michael and Poulos, Thomas L.},
abstractNote = {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.},
doi = {10.1073/pnas.1521664113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 5,
volume = 113,
place = {United States},
year = {2016},
month = {1}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1073/pnas.1521664113

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Cited by: 13 works
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