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:
-
- 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
- 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}
}
https://doi.org/10.1073/pnas.1521664113
Web of Science
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