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Resonance Raman Investigations of [NiFe] Hydrogenase Models

Behnke, Shelby Lee

Abstract Details

2016, Master of Science, Ohio State University, Chemistry.
Hydrogenase (H2ases) enzymes carry out bidirectional hydrogen production and oxidation reactions. To better understand the mechanism of hydrogen conversion, spectroscopic studies on small molecule mimics provide important metrics to correlate structure and function of the native enzymes. In this work, a series of molecular complexes that mimic the [NiFe] hydrogenase have been synthesized with different phosphine ligand substituents and analyzed using multiple analytical techniques, including nuclear magnetic resonance, Fourier transform infrared, and resonance Raman spectroscopies. Three model compounds have been selected as the focus of this investigation into the vibrational structure of the [NiFe] active site: [Ni(dppe)(µ-pdt)(µ-H)Fe(CO)3][BF4], [Ni(dcpe)(µ-pdt)(µ-H)Fe(CO)3][BF4], and [Ni(dppbz)(µ-pdt)(µ-H)Fe(CO)3][BF4]. (dppe= diphenylphosphinoethane, dcpe= dicyclohexylphosphinoethane, and dppbz= diphenylphosphinobenzene). These compounds have been previously synthesized and shown to exhibit high activity for proton reduction but have not been fully characterized spectroscopically to assess the solution-phase structure of the metal-hydride core. (Barton et al., 2010, JACS. 132, 14877-14885.) Specifically, resonance Raman (RR) spectroscopy was used to study the vibrational bands of each of the molecules, which were then assigned to specific normal modes of the molecule. The [Ni(dppe)(µ-pdt)(µ-H)Fe(CO)3]BF4 compound has been previously studied in great detail by RR, and this molecule was used as a template from which to understand the structures of the series. It was found that perturbations of ligands on the metal center alter the molecular vibrations, particularly of the metal-hydride core. This work provides important metrics for comparison between synthetic and the natural enzyme systems, with the intention of better understanding the mechanisms of native hydrogenases and informing next-generation catalyst design.
Hannah Shafaat, Dr. (Advisor)
Nagib David , Dr. (Committee Member)
68 p.

Recommended Citations

Citations

  • Behnke, S. L. (2016). Resonance Raman Investigations of [NiFe] Hydrogenase Models [Master's thesis, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1479728987893667

    APA Style (7th edition)

  • Behnke, Shelby. Resonance Raman Investigations of [NiFe] Hydrogenase Models. 2016. Ohio State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1479728987893667.

    MLA Style (8th edition)

  • Behnke, Shelby. "Resonance Raman Investigations of [NiFe] Hydrogenase Models." Master's thesis, Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1479728987893667

    Chicago Manual of Style (17th edition)