Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase

Ratzloff, Michael W.; Wilker, Molly B.; Mulder, David W.; Lubner, Carolyn E.; Hamby, Hayden; Brown, Katherine A.; Dukovic, Gordana; King, Paul W.

doi:10.1021/jacs.7b04216

Title: Activation Thermodynamics and H/D Kinetic Isotope Effect of the H_ox to H_red H⁺ Transition in [FeFe] Hydrogenase

Abstract

Molecular complexes between CdSe nanocrystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-driven control of electron transfer for spectroscopic detection of redox intermediates during catalytic proton reduction. Here in this paper we address the route of electron transfer from CdSe→CaI and activation thermodynamics of the initial step of proton reduction in CaI. The electron paramagnetic spectroscopy of illuminated CdSe:CaI showed how the CaI accessory FeS cluster chain (F-clusters) functions in electron transfer with CdSe. The H_ox→H_redH⁺ reduction step measured by Fourier-transform infrared spectroscopy showed an enthalpy of activation of 19 kJ mol^-1 and a ~2.5-fold kinetic isotope effect. Overall these results support electron injection from CdSe into CaI involving F-clusters, and that the H_ox→H_redH⁺ step of catalytic proton reduction in CaI proceeds by a proton-dependent process.

Authors:

Ratzloff, Michael W. ^[1]; Wilker, Molly B. ^[2]; Mulder, David W. ^[1];

^[1]; Hamby, Hayden ^[2]; Brown, Katherine A. ^[1];

^[2];

^[1]

National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center
Univ. of Colorado, Boulder, CO (United States). Dept. of Chemistry and Biochemistry

Publication Date:: Tue Aug 29 00:00:00 EDT 2017

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

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI Identifier:: 1394746

Report Number(s):: NREL/JA-2700-68424
Journal ID: ISSN 0002-7863; TRN: US1702385

Grant/Contract Number:: AC36-08GO28308; SC0010334

Resource Type:: Accepted Manuscript

Journal Name:: Journal of the American Chemical Society

Additional Journal Information:: Journal Volume: 139; Journal Issue: 37; Journal ID: ISSN 0002-7863

Publisher:: American Chemical Society (ACS)

Country of Publication:: United States

Language:: English

Subject:: 09 BIOMASS FUELS; thermodynamics; H2 catalysis; hydrogenase

Citation Formats


                    Ratzloff, Michael W., Wilker, Molly B., Mulder, David W., Lubner, Carolyn E., Hamby, Hayden, Brown, Katherine A., Dukovic, Gordana, and King, Paul W. Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase.  United States: N. p., 2017. 
Web.  doi:10.1021/jacs.7b04216.

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                    Ratzloff, Michael W., Wilker, Molly B., Mulder, David W., Lubner, Carolyn E., Hamby, Hayden, Brown, Katherine A., Dukovic, Gordana, & King, Paul W. Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase.  United States.  https://doi.org/10.1021/jacs.7b04216

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                    Ratzloff, Michael W., Wilker, Molly B., Mulder, David W., Lubner, Carolyn E., Hamby, Hayden, Brown, Katherine A., Dukovic, Gordana, and King, Paul W. Tue .  
"Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase".  United States.  https://doi.org/10.1021/jacs.7b04216.  https://www.osti.gov/servlets/purl/1394746.

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@article{osti_1394746,

  title        = {Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase},

  author       = {Ratzloff, Michael W. and Wilker, Molly B. and Mulder, David W. and Lubner, Carolyn E. and Hamby, Hayden and Brown, Katherine A. and Dukovic, Gordana and King, Paul W.},

  abstractNote = {Molecular complexes between CdSe nanocrystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-driven control of electron transfer for spectroscopic detection of redox intermediates during catalytic proton reduction. Here in this paper we address the route of electron transfer from CdSe→CaI and activation thermodynamics of the initial step of proton reduction in CaI. The electron paramagnetic spectroscopy of illuminated CdSe:CaI showed how the CaI accessory FeS cluster chain (F-clusters) functions in electron transfer with CdSe. The Hox→HredH+ reduction step measured by Fourier-transform infrared spectroscopy showed an enthalpy of activation of 19 kJ mol-1 and a ~2.5-fold kinetic isotope effect. Overall these results support electron injection from CdSe into CaI involving F-clusters, and that the Hox→HredH+ step of catalytic proton reduction in CaI proceeds by a proton-dependent process.},

  doi          = {10.1021/jacs.7b04216},

  journal      = {Journal of the American Chemical Society},

  number       = 37,

  volume       = 139,

  place        = {United States},

  year         = {Tue Aug 29 00:00:00 EDT 2017},

  month        = {Tue Aug 29 00:00:00 EDT 2017}

}

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Works referencing / citing this record:

Coupling biology to synthetic nanomaterials for semi-artificial photosynthesis
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Brown, Katherine A.; King, Paul W.
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Title: Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to Hred H+ Transition in [FeFe] Hydrogenase

Abstract

Citation Formats

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Identification of a Catalytic Iron-Hydride at the H-Cluster of [FeFe]-Hydrogenase journal, December 2016

Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases journal, January 2017

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Proton Transport in Clostridium pasteurianum [FeFe] Hydrogenase I: A Computational Study
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Reversible Carbon Monoxide Binding and Inhibition at the Active Site of the Fe-Only Hydrogenase ^†
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Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution
journal, January 2016

Frequency and potential dependence of reversible electrocatalytic hydrogen interconversion by [FeFe]-hydrogenases
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Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
journal, July 2012

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Theory of Proton-Coupled Electron Transfer in Energy Conversion Processes
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Isotopic fractionation associated with [NiFe]- and [FeFe]-hydrogenases: Isotopic fractionation associated with [NiFe]- and [FeFe]-hydrogenases
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