Chemistry & Biochemistry

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The Department of Chemistry and Biochemistry offers research-oriented programs culminating in the Doctor of Philosophy degree. The faculty in the department have expertise over a broad range of specialty areas including synthesis, structure, spectroscopy, and mechanism. In each of these fields, the strength of the department has been recognized at the international level.

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Author: search.filters.author.Fausset, Huntersearch.filters.applied.f.department: search.filters.department.Chemistry & Biochemistry.

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    Arsenic Exposure Causes Global Changes in the Metalloproteome of Escherichia coli
    (MDPI AG, 2023-02) Larson, James; Tokmina-Lukaszewska, Monika; Fausset, Hunter; Spurzem, Scott; Cox, Savannah; Cooper, Gwendolyn; Copié, Valérie; Bothner, Brian
    Arsenic is a toxic metalloid with differential biological effects, depending on speciation and concentration. Trivalent arsenic (arsenite, AsIII) is more toxic at lower concentrations than the pentavalent form (arsenate, AsV). In E. coli, the proteins encoded by the arsRBC operon are the major arsenic detoxification mechanism. Our previous transcriptional analyses indicate broad changes in metal uptake and regulation upon arsenic exposure. Currently, it is not known how arsenic exposure impacts the cellular distribution of other metals. This study examines the metalloproteome of E. coli strains with and without the arsRBC operon in response to sublethal doses of AsIII and AsV. Size exclusion chromatography coupled with inductively coupled plasma mass spectrometry (SEC-ICPMS) was used to investigate the distribution of five metals (56Fe, 24Mg, 66Zn, 75As, and 63Cu) in proteins and protein complexes under native conditions. Parallel analysis by SEC-UV-Vis spectroscopy monitored the presence of protein cofactors. Together, these data reveal global changes in the metalloproteome, proteome, protein cofactors, and soluble intracellular metal pools in response to arsenic stress in E. coli. This work brings to light one outcome of metal exposure and suggests that metal toxicity on the cellular level arises from direct and indirect effects.
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    Proteomic Analysis of Methanococcus voltae Grown in the Presence of Mineral and Nonmineral Sources of Iron and Sulfur
    (American Society for Microbiology, 2022-08) Steward, Katherine F.; Payne, Devon; Kincannon, Will; Johnson, Christina; Lensing, Malachi; Fausset, Hunter; Németh, Brigitta; Shepard, Eric M.; Broderick, William E.; Broderick, Joan B.; Dubois, Jen; Bothner, Brian
    Clusters of iron and sulfur are key components of the active sites of enzymes that facilitate microbial conversion of light or electrical energy into chemical bonds. The proteins responsible for transporting iron and sulfur into cells and assembling these elements into metal clusters are not well understood.
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