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Title: Chapter 2: Structure-Function of [FeFe]- and [NiFe]-Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation

Abstract

[FeFe]- and [NiFe]-hydrogenases are two classes of enzymes that couple the reversible reduction of protons to the production of hydrogen gas. While these enzymes have unique taxonomic distributions and differences in their structure, function, maturation, and evolutionary history, they nevertheless share important similarities and may both be of critical importance for photobiological hydrogen production. Here, the structural and functional diversity of both types of hydrogenases are discussed in light of their phylogenetic and metabolic contexts. Overviews of the mechanisms of hydrogen activation at the respective active sites are given and provide insight into the role of the surrounding protein coordination sphere in catalysis and tuning reactivity. The distinct maturation pathways of both the [FeFe]- and [NiFe]-hydrogenases are described, revealing unique processes for assembling diatomic carbon monoxide and cyanide ligands onto Fe atoms, a key feature of the active sites that facilitates hydrogen activation during turnover conditions. Finally, a discussion of bifurcating [FeFe]- and [NiFe]-hydrogenases sheds light on this recently characterized group of enzymes that may hold a profound advantage at energetically efficient hydrogen production.

Authors:
ORCiD logo [1];  [1];  [2];  [3];  [3];  [4];  [5];  [5];  [4];  [3];  [3]
  1. National Renewable Energy Laboratory (NREL), Golden, CO (United States)
  2. Washington State University
  3. Montana State University
  4. University of Georgia
  5. Arizona State University
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:
1471175
Report Number(s):
NREL/CH-2700-68483
DOE Contract Number:  
AC36-08GO28308
Resource Type:
Book
Country of Publication:
United States
Language:
English
Subject:
08 HYDROGEN; 09 BIOMASS FUELS; [FeFe]-hydrogenases; enzymes; hydrogen production

Citation Formats

King, Paul W, Mulder, David W, Artz, Jacob H., Poudel, Saroj, Colman, Daniel, Schut, Gerrit J., Williams, Garrett, Jones, Anne K., Adams, Michael W. W., Boyd, Eric S., and Peters, John W. Chapter 2: Structure-Function of [FeFe]- and [NiFe]-Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation. United States: N. p., 2018. Web. doi:10.1039/9781849737128-00031.
King, Paul W, Mulder, David W, Artz, Jacob H., Poudel, Saroj, Colman, Daniel, Schut, Gerrit J., Williams, Garrett, Jones, Anne K., Adams, Michael W. W., Boyd, Eric S., & Peters, John W. Chapter 2: Structure-Function of [FeFe]- and [NiFe]-Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation. United States. doi:10.1039/9781849737128-00031.
King, Paul W, Mulder, David W, Artz, Jacob H., Poudel, Saroj, Colman, Daniel, Schut, Gerrit J., Williams, Garrett, Jones, Anne K., Adams, Michael W. W., Boyd, Eric S., and Peters, John W. Tue . "Chapter 2: Structure-Function of [FeFe]- and [NiFe]-Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation". United States. doi:10.1039/9781849737128-00031.
@article{osti_1471175,
title = {Chapter 2: Structure-Function of [FeFe]- and [NiFe]-Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation},
author = {King, Paul W and Mulder, David W and Artz, Jacob H. and Poudel, Saroj and Colman, Daniel and Schut, Gerrit J. and Williams, Garrett and Jones, Anne K. and Adams, Michael W. W. and Boyd, Eric S. and Peters, John W.},
abstractNote = {[FeFe]- and [NiFe]-hydrogenases are two classes of enzymes that couple the reversible reduction of protons to the production of hydrogen gas. While these enzymes have unique taxonomic distributions and differences in their structure, function, maturation, and evolutionary history, they nevertheless share important similarities and may both be of critical importance for photobiological hydrogen production. Here, the structural and functional diversity of both types of hydrogenases are discussed in light of their phylogenetic and metabolic contexts. Overviews of the mechanisms of hydrogen activation at the respective active sites are given and provide insight into the role of the surrounding protein coordination sphere in catalysis and tuning reactivity. The distinct maturation pathways of both the [FeFe]- and [NiFe]-hydrogenases are described, revealing unique processes for assembling diatomic carbon monoxide and cyanide ligands onto Fe atoms, a key feature of the active sites that facilitates hydrogen activation during turnover conditions. Finally, a discussion of bifurcating [FeFe]- and [NiFe]-hydrogenases sheds light on this recently characterized group of enzymes that may hold a profound advantage at energetically efficient hydrogen production.},
doi = {10.1039/9781849737128-00031},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2018},
month = {3}
}

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