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

Abstract

Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur 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.

Authors:
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [2]; ORCiD logo [2];  [1]
  1. Florida State Univ., Tallahassee, FL (United States). Institute of Molecular Biophysics
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1784132
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Structural Biology
Additional Journal Information:
Journal Volume: 213; Journal Issue: 2; Journal ID: ISSN 1047-8477
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Analytical ultracentrifugation; Assimilatory NADPH-dependent sulfite reductase; Electron transfer; Oxidoreductase; Solution scattering

Citation Formats

Murray, Daniel T., Weiss, Kevin L., Stanley, Christopher B., Nagy, Gergely, and Stroupe, Margaret Elizabeth. Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase. United States: N. p., 2021. Web. doi:10.1016/j.jsb.2021.107724.
Murray, Daniel T., Weiss, Kevin L., Stanley, Christopher B., Nagy, Gergely, & Stroupe, Margaret Elizabeth. Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase. United States. https://doi.org/10.1016/j.jsb.2021.107724
Murray, Daniel T., Weiss, Kevin L., Stanley, Christopher B., Nagy, Gergely, and Stroupe, Margaret Elizabeth. Tue . "Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase". United States. https://doi.org/10.1016/j.jsb.2021.107724. https://www.osti.gov/servlets/purl/1784132.
@article{osti_1784132,
title = {Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase},
author = {Murray, Daniel T. and Weiss, Kevin L. and Stanley, Christopher B. and Nagy, Gergely and Stroupe, Margaret Elizabeth},
abstractNote = {Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur 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.},
doi = {10.1016/j.jsb.2021.107724},
journal = {Journal of Structural Biology},
number = 2,
volume = 213,
place = {United States},
year = {Tue Jun 01 00:00:00 EDT 2021},
month = {Tue Jun 01 00:00:00 EDT 2021}
}

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