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Applications of resonance Raman spectroscopy to the study of bioinorganic macromolecules

Maugeri, Pearson Thomas, Maugeri
http://orcid.org/0000-0002-6755-4310
http://rave.ohiolink.edu/etdc/view?acc_num=osu1512093478871388

Abstract Details

2017, Doctor of Philosophy, Ohio State University, Biophysics.
Metalloproteins are essential to life, with roles in cellular signaling, metabolism, gas cycles, and gene regulation, among others. One group of metalloproteins is the ferritin-like superfamily, which contains a wide variety of members ranging from iron-trafficking proteins (ferritin) to enzymes that can perform 2-electron chemistry on hydrocarbons (bacterial multicomponent monooxygenases or BMMs). Ribonucleotide reductases (RNRs), one of the members of the ferritin-like superfamily, are enzymes that catalyze the only known de novo reduction of ribonucleotides to deoxyribonucleotides and are found is nearly every organism on earth. Recently, a novel protein was discovered in Mycobacterium tuberculosis called R2lox, because of its sequence similarity to the R2 subunit of RNR, whose function remains unknown. However, it does not possess any RNR activity and is more similar in active site structure and proposed function to the BMMs. This protein is very important from a basic science standpoint as well as a health science standpoint because of its unique metal-binding capabilities and because it is upregulated in the virulent H37rv strain of M. tuberculosis. To study the active site structure and oxygen activation reaction of this protein, a custom resonance Raman spectroscopic system was designed and built. This system is very versatile in that it can access many different wavelengths with a single laser, which is useful for resonance Raman, which relies on tuning the Raman excitation beam to an electronic absorption to enhance the scattering efficiency of Raman light. In addition to R2lox, this custom resonance Raman system has been used on numerous bioinorganic molecules to great effect. This work describes the design and construction of the custom resonance Raman system and its use in studying R2lox and other bioinorganic systems. Additionally, experiments were performed to lay the groundwork for studying electron transfer in R2lox via ruthenium modification.
Hannah Shafaat, PhD (Advisor)
James Cowan, PhD (Committee Member)
Terry Gustafson, PhD (Committee Member)
Marcos Sotomayor, PhD (Committee Member)
221 p.
Chemistry
Bioinorganic chemistry; spectroscopy; resonance Raman spectroscopy; lasers; nonlinear optics; ferritin-like superfamily; R2lox; photoinduced processes; electron transfer

Recommended Citations

Citations

  • Maugeri, Maugeri, P. T. (2017). Applications of resonance Raman spectroscopy to the study of bioinorganic macromolecules [Doctoral dissertation, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1512093478871388

    APA Style (7th edition)

  • Maugeri, Maugeri, Pearson. Applications of resonance Raman spectroscopy to the study of bioinorganic macromolecules. 2017. Ohio State University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1512093478871388.

    MLA Style (8th edition)

  • Maugeri, Maugeri, Pearson. "Applications of resonance Raman spectroscopy to the study of bioinorganic macromolecules." Doctoral dissertation, Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1512093478871388

    Chicago Manual of Style (17th edition)

osu1512093478871388
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This open access ETD is published by The Ohio State University and OhioLINK.