Structure and function of photosystem I–[FeFe] hydrogenase protein fusions: An all-atom molecular dynamics study
Abstract
All-atom molecular dynamics (MD) simulation was used to study the solution dynamics and protein protein interactions of protein fusions of photosystem I (PSI) from Thermosynechococcus elongatus and an [FeFe]-hydrogenase (FeFe H2ase) from Clostridium pasteurianum, a unique complex capable of photocatalytic hydrogen production. This study involved fusions of these two proteins via dithiol linkers of different length including decanedithiol, octanedithiol, and hexanedithiol, for which experimental data had previously been obtained. Evaluation of root-mean-squared deviations (RMSDs) relative to the respective crystal structures of PSI and the FeFe H2ase shows that these fusion complexes approach stable equilibrium conformations during the MD simulations. Investigating protein mobility via root-mean-squared fluctuations (RMSFs) reveals that tethering via the shortest hexanedithiol linker results in increased atomic fluctuations of both PSI and the hydrogenase in these fusion complexes. Furthermore, evaluation of the inter- and intraprotein electron transfer distances in these fusion complexes indicates that the structural changes in the FeFe H2ase arising from ligation to PSI via the shortest hexanedithiol linker may hinder electron transport in the hydrogenase, thus providing a molecular level explanation for the observation that the medium-length octanedithiol linker gives the highest hydrogen production rate.
- Authors:
-
- Univ. of Tennessee, Knoxville, TN (United States)
- Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1327649
- Grant/Contract Number:
- AC05-00OR22725
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry
- Additional Journal Information:
- Journal Volume: 120; Journal Issue: 4; Journal ID: ISSN 1520-6106
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; photosystem I; hydrogenase; membrane proteins; molecular dynamics
Citation Formats
Harris, Bradley J., Cheng, Xiaolin, and Frymier, Paul. Structure and function of photosystem I–[FeFe] hydrogenase protein fusions: An all-atom molecular dynamics study. United States: N. p., 2015.
Web. doi:10.1021/acs.jpcb.5b07812.
Harris, Bradley J., Cheng, Xiaolin, & Frymier, Paul. Structure and function of photosystem I–[FeFe] hydrogenase protein fusions: An all-atom molecular dynamics study. United States. https://doi.org/10.1021/acs.jpcb.5b07812
Harris, Bradley J., Cheng, Xiaolin, and Frymier, Paul. Tue .
"Structure and function of photosystem I–[FeFe] hydrogenase protein fusions: An all-atom molecular dynamics study". United States. https://doi.org/10.1021/acs.jpcb.5b07812. https://www.osti.gov/servlets/purl/1327649.
@article{osti_1327649,
title = {Structure and function of photosystem I–[FeFe] hydrogenase protein fusions: An all-atom molecular dynamics study},
author = {Harris, Bradley J. and Cheng, Xiaolin and Frymier, Paul},
abstractNote = {All-atom molecular dynamics (MD) simulation was used to study the solution dynamics and protein protein interactions of protein fusions of photosystem I (PSI) from Thermosynechococcus elongatus and an [FeFe]-hydrogenase (FeFe H2ase) from Clostridium pasteurianum, a unique complex capable of photocatalytic hydrogen production. This study involved fusions of these two proteins via dithiol linkers of different length including decanedithiol, octanedithiol, and hexanedithiol, for which experimental data had previously been obtained. Evaluation of root-mean-squared deviations (RMSDs) relative to the respective crystal structures of PSI and the FeFe H2ase shows that these fusion complexes approach stable equilibrium conformations during the MD simulations. Investigating protein mobility via root-mean-squared fluctuations (RMSFs) reveals that tethering via the shortest hexanedithiol linker results in increased atomic fluctuations of both PSI and the hydrogenase in these fusion complexes. Furthermore, evaluation of the inter- and intraprotein electron transfer distances in these fusion complexes indicates that the structural changes in the FeFe H2ase arising from ligation to PSI via the shortest hexanedithiol linker may hinder electron transport in the hydrogenase, thus providing a molecular level explanation for the observation that the medium-length octanedithiol linker gives the highest hydrogen production rate.},
doi = {10.1021/acs.jpcb.5b07812},
journal = {Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry},
number = 4,
volume = 120,
place = {United States},
year = {Tue Dec 15 00:00:00 EST 2015},
month = {Tue Dec 15 00:00:00 EST 2015}
}
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