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Title: Merging [FeFe]-Hydrogenases with Materials and Nanomaterials as Biohybrid Catalysts for Solar H2 Production

Abstract

The catalysts commonly used for the H{sub 2} producing reaction in artificial solar systems are typically platinum or particulate platinum composites. Biological catalysts, the hydrogenases, exist in a wide-variety of microbes and are biosynthesized from abundant, non-precious metals. By virtue of a unique catalytic metallo-cluster that is composed of iron and sulfur, [FeFe]-hydrogenases are capable of catalyzing H{sub 2} production at turnover rates of millimoles-per-second. In addition, these biological catalysts possess some of the characteristics that are desired for cost-effective solar H{sub 2} production systems, high solubilities in aqueous solutions and low activation energies, but are sensitive to CO and O{sub 2}. We are investigating ways to merge [FeFe]-hydrogenases with a variety of organic materials and nanomaterials for the fabrication of electrodes and biohybrids as catalysts for use in artificial solar H{sub 2} production systems. These efforts include designs that allow for the integration of [FeFe]-hydrogenase in dye-solar cells as models to measure solar conversion and H{sub 2} production efficiencies. In support of a more fundamental understanding of [FeFe]-hydrogenase for these and other applications the role of protein structure in catalysis is being investigated. Currently there is little known about the mechanism of how these and other enzymes couple multi-electronmore » transfer to proton reduction. To further the mechanistic understanding of [FeFe]-hydrogenases, structural models for substrate transfer are being used to create enzyme variants for biochemical analysis. Here results are presented on investigations of proton-transfer pathways in [FeFe]-hydrogenase and their interaction with single-walled carbon nanotubes.« less

Authors:
; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
940622
DOE Contract Number:
AC36-99-GO10337
Resource Type:
Journal Article
Resource Relation:
Journal Name: Solar Hydrogen and Nanotechnology II; Journal Volume: 6650
Country of Publication:
United States
Language:
English
Subject:
08 HYDROGEN; 14 SOLAR ENERGY; 36 MATERIALS SCIENCE; 77 NANOSCIENCE AND NANOTECHNOLOGY; AQUEOUS SOLUTIONS; CARBON; CATALYSIS; CATALYSTS; ELECTRODES; ENZYMES; FABRICATION; HYDROGEN; HYDROGENASES; IRON; NANOTUBES; PARTICULATES; PLATINUM; PROTEIN STRUCTURE; PROTONS; SOLAR SYSTEM; STRUCTURAL MODELS; SUBSTRATES; SULFUR; Basic Sciences

Citation Formats

King, P. W., Svedruzic, D., Hambourger, M., Gervaldo, M., McDonald, T., Blackburn, J., Heben, M., Gust, D., Moore, A. L., Moore, T. A., and Ghirardi, M. L.. Merging [FeFe]-Hydrogenases with Materials and Nanomaterials as Biohybrid Catalysts for Solar H2 Production. United States: N. p., 2007. Web. doi:10.1117/12.736556.
King, P. W., Svedruzic, D., Hambourger, M., Gervaldo, M., McDonald, T., Blackburn, J., Heben, M., Gust, D., Moore, A. L., Moore, T. A., & Ghirardi, M. L.. Merging [FeFe]-Hydrogenases with Materials and Nanomaterials as Biohybrid Catalysts for Solar H2 Production. United States. doi:10.1117/12.736556.
King, P. W., Svedruzic, D., Hambourger, M., Gervaldo, M., McDonald, T., Blackburn, J., Heben, M., Gust, D., Moore, A. L., Moore, T. A., and Ghirardi, M. L.. Mon . "Merging [FeFe]-Hydrogenases with Materials and Nanomaterials as Biohybrid Catalysts for Solar H2 Production". United States. doi:10.1117/12.736556.
@article{osti_940622,
title = {Merging [FeFe]-Hydrogenases with Materials and Nanomaterials as Biohybrid Catalysts for Solar H2 Production},
author = {King, P. W. and Svedruzic, D. and Hambourger, M. and Gervaldo, M. and McDonald, T. and Blackburn, J. and Heben, M. and Gust, D. and Moore, A. L. and Moore, T. A. and Ghirardi, M. L.},
abstractNote = {The catalysts commonly used for the H{sub 2} producing reaction in artificial solar systems are typically platinum or particulate platinum composites. Biological catalysts, the hydrogenases, exist in a wide-variety of microbes and are biosynthesized from abundant, non-precious metals. By virtue of a unique catalytic metallo-cluster that is composed of iron and sulfur, [FeFe]-hydrogenases are capable of catalyzing H{sub 2} production at turnover rates of millimoles-per-second. In addition, these biological catalysts possess some of the characteristics that are desired for cost-effective solar H{sub 2} production systems, high solubilities in aqueous solutions and low activation energies, but are sensitive to CO and O{sub 2}. We are investigating ways to merge [FeFe]-hydrogenases with a variety of organic materials and nanomaterials for the fabrication of electrodes and biohybrids as catalysts for use in artificial solar H{sub 2} production systems. These efforts include designs that allow for the integration of [FeFe]-hydrogenase in dye-solar cells as models to measure solar conversion and H{sub 2} production efficiencies. In support of a more fundamental understanding of [FeFe]-hydrogenase for these and other applications the role of protein structure in catalysis is being investigated. Currently there is little known about the mechanism of how these and other enzymes couple multi-electron transfer to proton reduction. To further the mechanistic understanding of [FeFe]-hydrogenases, structural models for substrate transfer are being used to create enzyme variants for biochemical analysis. Here results are presented on investigations of proton-transfer pathways in [FeFe]-hydrogenase and their interaction with single-walled carbon nanotubes.},
doi = {10.1117/12.736556},
journal = {Solar Hydrogen and Nanotechnology II},
number = ,
volume = 6650,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}