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Title: Unification of [FeFe]-hydrogenases into three structural and functional groups

Abstract

[FeFe]-hydrogenases (Hyd) are structurally diverse enzymes that catalyze the reversible oxidation of hydrogen (H 2). Recent biochemical data demonstrate new functional roles for these enzymes, including those that function in electron bifurcation where an exergonic reaction is coupled with an endergonic reaction to drive the reversible oxidation/production of H 2. To identify the structural determinants that underpin differences in enzyme functionality, a total of 714 homologous sequences of the catalytic subunit, HydA, were compiled. Bioinformatics approaches informed by biochemical data were then used to characterize differences in inferred quaternary structure, HydA active site protein environment, accessory iron-sulfur clusters in HydA, and regulatory proteins encoded in HydA gene neighborhoods. HydA homologs were clustered into one of three classification groups, Group 1 (G1), Group 2 (G2), and Group 3 (G3). G1 enzymes were predicted to be monomeric while those in G2 and G3 were predicted to be multimeric and include HydB, HydC (G2/G3) and HydD (G3) subunits. Variation in the HydA active site and accessory iron-sulfur clusters did not vary by group type. Group-specific regulatory genes were identified in the gene neighborhoods of both G2 and G3 Hyd. Analyses of purified G2 and G3 enzymes by mass spectrometry strongly suggests that theymore » are post-translationally modified by phosphorylation. In conclusion, these results suggest that bifurcation capability is dictated primarily by the presence of both HydB and HydC in Hyd complexes, rather than by variation in HydA.« less

Authors:
 [1];  [1];  [1];  [1];  [2];  [3];  [3];  [2];  [1];  [1];  [1]
  1. Montana State Univ., Bozeman, MT (United States)
  2. Univ. of Georgia, Athens, GA (United States)
  3. National Renewable Energy Lab. (NREL), Golden, CO (United States)
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1257943
Alternate Identifier(s):
OSTI ID: 1358821
Report Number(s):
NREL/JA-2700-66632
Journal ID: ISSN 0304-4165
Grant/Contract Number:  
SC0012518; AC36-08GO28308; 5P20RR02437
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biochimica et Biophysica Acta - General Subjects
Additional Journal Information:
Journal Volume: 1860; Journal Issue: 9; Journal ID: ISSN 0304-4165
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; [FeFe]-hydrogenase; hydrogen; electron bifurcation; post-translational modification; regulation; bioinformatics

Citation Formats

Poudel, Saroj, Tokmina-Lukaszewska, Monika, Colman, Daniel R., Refai, Mohammed, Schut, Gerrit J., King, Paul W., Maness, Pin-Ching, Adams, Michael W. W., Peters, John W., Bothner, Brian, and Boyd, Eric S. Unification of [FeFe]-hydrogenases into three structural and functional groups. United States: N. p., 2016. Web. doi:10.1016/j.bbagen.2016.05.034.
Poudel, Saroj, Tokmina-Lukaszewska, Monika, Colman, Daniel R., Refai, Mohammed, Schut, Gerrit J., King, Paul W., Maness, Pin-Ching, Adams, Michael W. W., Peters, John W., Bothner, Brian, & Boyd, Eric S. Unification of [FeFe]-hydrogenases into three structural and functional groups. United States. doi:10.1016/j.bbagen.2016.05.034.
Poudel, Saroj, Tokmina-Lukaszewska, Monika, Colman, Daniel R., Refai, Mohammed, Schut, Gerrit J., King, Paul W., Maness, Pin-Ching, Adams, Michael W. W., Peters, John W., Bothner, Brian, and Boyd, Eric S. Fri . "Unification of [FeFe]-hydrogenases into three structural and functional groups". United States. doi:10.1016/j.bbagen.2016.05.034. https://www.osti.gov/servlets/purl/1257943.
@article{osti_1257943,
title = {Unification of [FeFe]-hydrogenases into three structural and functional groups},
author = {Poudel, Saroj and Tokmina-Lukaszewska, Monika and Colman, Daniel R. and Refai, Mohammed and Schut, Gerrit J. and King, Paul W. and Maness, Pin-Ching and Adams, Michael W. W. and Peters, John W. and Bothner, Brian and Boyd, Eric S.},
abstractNote = {[FeFe]-hydrogenases (Hyd) are structurally diverse enzymes that catalyze the reversible oxidation of hydrogen (H2). Recent biochemical data demonstrate new functional roles for these enzymes, including those that function in electron bifurcation where an exergonic reaction is coupled with an endergonic reaction to drive the reversible oxidation/production of H2. To identify the structural determinants that underpin differences in enzyme functionality, a total of 714 homologous sequences of the catalytic subunit, HydA, were compiled. Bioinformatics approaches informed by biochemical data were then used to characterize differences in inferred quaternary structure, HydA active site protein environment, accessory iron-sulfur clusters in HydA, and regulatory proteins encoded in HydA gene neighborhoods. HydA homologs were clustered into one of three classification groups, Group 1 (G1), Group 2 (G2), and Group 3 (G3). G1 enzymes were predicted to be monomeric while those in G2 and G3 were predicted to be multimeric and include HydB, HydC (G2/G3) and HydD (G3) subunits. Variation in the HydA active site and accessory iron-sulfur clusters did not vary by group type. Group-specific regulatory genes were identified in the gene neighborhoods of both G2 and G3 Hyd. Analyses of purified G2 and G3 enzymes by mass spectrometry strongly suggests that they are post-translationally modified by phosphorylation. In conclusion, these results suggest that bifurcation capability is dictated primarily by the presence of both HydB and HydC in Hyd complexes, rather than by variation in HydA.},
doi = {10.1016/j.bbagen.2016.05.034},
journal = {Biochimica et Biophysica Acta - General Subjects},
issn = {0304-4165},
number = 9,
volume = 1860,
place = {United States},
year = {2016},
month = {5}
}

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