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Title: Chapter Eight - Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases

Abstract

The crystallization of FeS cluster-containing proteins has been challenging due to their oxygen sensitivity, and yet these enzymes are involved in many critical catalytic reactions. The last few years have seen a wealth of innovative experiments designed to elucidate not just structural but mechanistic insights into FeS cluster enzymes. Here, we focus on the crystallization of hydrogenases, which catalyze the reversible reduction of protons to hydrogen, and nitrogenases, which reduce dinitrogen to ammonia. A specific focus is given to the different experimental parameters and strategies that are used to trap distinct enzyme states, specifically, oxidants, reductants, and gas-treatments. Other themes presented here include the recent use of Cryo-EM, and how coupling various spectroscopies to crystallization is opening up new approaches for structural and mechanistic analysis.

Authors:
ORCiD logo [1];  [1];  [2];  [2];  [2]
  1. National Renewable Energy Laboratory (NREL), Golden, CO (United States)
  2. Washington State University
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States); Energy Frontier Research Centers (EFRC) (United States). Center for Biological Electron Transfer and Catalysis (BETCy)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1389733
Report Number(s):
NREL/CH-2700-68449
Journal ID: ISSN 0076-6879
DOE Contract Number:  
AC36-08GO28308
Resource Type:
Journal Article
Resource Relation:
Journal Name: Methods in Enzymology; Journal Volume: 595
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; hydrogenase; nitrogenases; crystallography; FeS clusters; oxygen sensitive

Citation Formats

King, Paul W, Mulder, David W, Artz, Jacob H., Zadvornyy, Oleg A., and Peters, John W. Chapter Eight - Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases. United States: N. p., 2017. Web. doi:10.1016/bs.mie.2017.07.005.
King, Paul W, Mulder, David W, Artz, Jacob H., Zadvornyy, Oleg A., & Peters, John W. Chapter Eight - Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases. United States. doi:10.1016/bs.mie.2017.07.005.
King, Paul W, Mulder, David W, Artz, Jacob H., Zadvornyy, Oleg A., and Peters, John W. Mon . "Chapter Eight - Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases". United States. doi:10.1016/bs.mie.2017.07.005.
@article{osti_1389733,
title = {Chapter Eight - Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases},
author = {King, Paul W and Mulder, David W and Artz, Jacob H. and Zadvornyy, Oleg A. and Peters, John W.},
abstractNote = {The crystallization of FeS cluster-containing proteins has been challenging due to their oxygen sensitivity, and yet these enzymes are involved in many critical catalytic reactions. The last few years have seen a wealth of innovative experiments designed to elucidate not just structural but mechanistic insights into FeS cluster enzymes. Here, we focus on the crystallization of hydrogenases, which catalyze the reversible reduction of protons to hydrogen, and nitrogenases, which reduce dinitrogen to ammonia. A specific focus is given to the different experimental parameters and strategies that are used to trap distinct enzyme states, specifically, oxidants, reductants, and gas-treatments. Other themes presented here include the recent use of Cryo-EM, and how coupling various spectroscopies to crystallization is opening up new approaches for structural and mechanistic analysis.},
doi = {10.1016/bs.mie.2017.07.005},
journal = {Methods in Enzymology},
number = ,
volume = 595,
place = {United States},
year = {Mon Aug 21 00:00:00 EDT 2017},
month = {Mon Aug 21 00:00:00 EDT 2017}
}