Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes

doi:10.1117/12.736232

Title: Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes

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Abstract

Single-walled carbon nanotubes (SWNT) are promising candidates for use in energy conversion devices as an active photo-collecting elements, for dissociation of bound excitons and charge-transfer from photo-excited chromophores, or as molecular wires to transport charge. Hydrogenases are enzymes that efficiently catalyze the reduction of protons from a variety of electron donors to produce molecular hydrogen. Hydrogenases together with SWNT suggest a novel biohybrid material for direct conversion of sunlight into H{sub 2}. Here, we report changes in SWNT optical properties upon addition of recombinant [FeFe] hydrogenases from Clostridium acetobutylicum and Chlamydomonas reinhardtii. We find evidence that novel and stable charge-transfer complexes are formed under conditions of the hydrogenase catalytic turnover, providing spectroscopic handles for further study and application of this hybrid system.

Authors:: Chang, D. S.; McDonald, T. J.; Kim, Y.-H.; Blackburn, J. L.; Heben, M. J.; King, P. W.

Publication Date:: Mon Jan 01 00:00:00 EST 2007

Research Org.:: National Renewable Energy Lab. (NREL), Golden, CO (United States)

Sponsoring Org.:: USDOE

OSTI Identifier:: 940621

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; 09 BIOMASS FUELS; 77 NANOSCIENCE AND NANOTECHNOLOGY; BINDING ENERGY; CARBON; CHLAMYDOMONAS; CLOSTRIDIUM ACETOBUTYLICUM; DISSOCIATION; ELECTRONS; ENERGY CONVERSION; ENZYMES; EXCITONS; HYBRID SYSTEMS; HYDROGEN; HYDROGENASES; NANOTUBES; OPTICAL PROPERTIES; PROTONS; VALENCE; Basic Sciences

Citation Formats


                    Chang, D. S., McDonald, T. J., Kim, Y.-H., Blackburn, J. L., Heben, M. J., and King, P. W.. Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes.  United States: N. p., 2007. 
        Web.  doi:10.1117/12.736232.

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                    Chang, D. S., McDonald, T. J., Kim, Y.-H., Blackburn, J. L., Heben, M. J., & King, P. W.. Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes.  United States.  doi:10.1117/12.736232.

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                    Chang, D. S., McDonald, T. J., Kim, Y.-H., Blackburn, J. L., Heben, M. J., and King, P. W.. Mon .  
        "Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes".  United States.  
        doi:10.1117/12.736232.

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@article{osti_940621,

  title        = {Interaction of [FeFe]-Hydrogenases with Single-walled Carbon Nanotubes},

  author       = {Chang, D. S. and McDonald, T. J. and Kim, Y.-H. and Blackburn, J. L. and Heben, M. J. and King, P. W.},

  abstractNote = {Single-walled carbon nanotubes (SWNT) are promising candidates for use in energy conversion devices as an active photo-collecting elements, for dissociation of bound excitons and charge-transfer from photo-excited chromophores, or as molecular wires to transport charge. Hydrogenases are enzymes that efficiently catalyze the reduction of protons from a variety of electron donors to produce molecular hydrogen. Hydrogenases together with SWNT suggest a novel biohybrid material for direct conversion of sunlight into H{sub 2}. Here, we report changes in SWNT optical properties upon addition of recombinant [FeFe] hydrogenases from Clostridium acetobutylicum and Chlamydomonas reinhardtii. We find evidence that novel and stable charge-transfer complexes are formed under conditions of the hydrogenase catalytic turnover, providing spectroscopic handles for further study and application of this hybrid system.},

  doi          = {10.1117/12.736232},

  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}

}

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DOI: 10.1117/12.736232

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