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Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase

Daniel T. Murray, Kevin L. Weiss, Christopher B. Stanley, Gergely Nagy, View ORCID ProfileM. Elizabeth Stroupe
doi: https://doi.org/10.1101/2020.12.08.415968
Daniel T. Murray
1Department of Biological Science and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, 32306, USA
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Kevin L. Weiss
2Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, 37830, USA
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Christopher B. Stanley
2Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, 37830, USA
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Gergely Nagy
2Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, 37830, USA
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M. Elizabeth Stroupe
1Department of Biological Science and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, 32306, USA
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  • ORCID record for M. Elizabeth Stroupe
  • For correspondence: mestroupe@bio.fsu.edu
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ABSTRACT

Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur reduction for biomass incorporation. Electron transfer within SiR requires intra- and inter-subunit interactions that are mediated by the relative position of each protein, governed by flexible domain movements. Using small-angle neutron scattering, we report the first solution structures of SiR heterodimers containing a single copy of each subunit. These structures show how the subunits bind and how both subunit binding and oxidation state impact SiRFP’s conformation. Neutron contrast matching experiments on selectively deuterated heterodimers allow us to define the contribution of each subunit to the solution scattering. SiRHP binding induces a change in the position of SiRFP’s flavodoxin-like domain relative to its ferredoxin-NADP+ reductase domain while compacting SiRHP’s N-terminus. Reduction of SiRFP leads to a more open structure relative to its oxidized state, re-positioning SiRFP’s N-terminal flavodoxin-like domain towards the SiRHP binding position. These structures show, for the first time, how both SiRHP binding to, and reduction of, SiRFP positions SiRFP for electron transfer between the subunits.

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  • The authors declare that they have no conflict of interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted December 08, 2020.
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Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase
Daniel T. Murray, Kevin L. Weiss, Christopher B. Stanley, Gergely Nagy, M. Elizabeth Stroupe
bioRxiv 2020.12.08.415968; doi: https://doi.org/10.1101/2020.12.08.415968
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Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase
Daniel T. Murray, Kevin L. Weiss, Christopher B. Stanley, Gergely Nagy, M. Elizabeth Stroupe
bioRxiv 2020.12.08.415968; doi: https://doi.org/10.1101/2020.12.08.415968

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