Adjunct Assistant Professor, Department of Biomedical Sciences
Biosketch
Frederick Stull, PhD, is an assistant professor in the Department of Chemistry at Western Michigan University. He graduated from the University of South Florida, Tampa, Florida. He earned his doctorate in chemical biology from the University of Michigan, Ann Arbor, Michigan. The overarching goal of Dr. Stull's research is to understand how enzymes control catalysis. The Stull lab primarily focuses on the class of enzymes that use riboflavin-derived cofactors (flavin-dependent enzymes), which catalyze various chemical transformations crucial for life. Enzyme-bound flavin cofactors have spectroscopic signals that directly report on the chemistry occurring in the active site, which Stull's lab exploits to study their reaction mechanisms using transient kinetics. The Stull lab also uses directed evolution and protein engineering to transform nature's catalysts into useful tools for biotechnology/medical applications.
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Education and Training
- Postdoctoral Fellowship 2019, Chemical Biology, Howard Hughes Medical Institute
- PhD 2014, Chemical Biology, University of Michigan
- BS 2009, Chemistry, University of South Florida
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Research
- Protein Engineering
- Enzyme Catalysis
- Directed Molecular Evolution
- Biotechnology
- Biomedical applications
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Publications
Javanshad R., Taylor C.J., Delavari N., Barkman T.J., Stull F., Venter A.R. Analysis of histidine-tagged recombinant proteins from nickel and copper coated surfaces by direct electrospray ionization and desorption electrospray ionization mass spectrometry Rapid Communications in Mass Spectrometry. 2023;37
Choudhary V., Wu K., Zhang Z., Dulchavsky M., Barkman T., Bardwell J.C.A., Stull F. The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase Journal of Biological Chemistry. 2022;298(8)
Matthews A., Schönfelder J., Lagies S., Schleicher E., Kammerer B., Ellis H.R., Stull F., Teufel R. Bacterial flavoprotein monooxygenase YxeK salvages toxic S-(2-succino)-adducts via oxygenolytic C–S bond cleavage FEBS Journal. 2022;289(3):787-807.
Meredith J.D., Chapman I., Ulrich K., Sebastian C., Stull F., Gray M.J. Escherichia coli RclA is a highly active hypothiocyanite reductase Proceedings of the National Academy of Sciences of the United States of America. 2022;119(30)
Mumby E.J., Willoughby J.A., Vasquez C., Delavari N., Zhang Z., Clark C.T., Stull F. Binding Interface and Electron Transfer between Nicotine Oxidoreductase and Its Cytochrome c Electron Acceptor Biochemistry. 2022;61(20):2182-2187.
Bou-Nader C., Stull F.W., Pecqueur L., Simon P., Guérineau V., Royant A., Fontecave M., Lombard M., Palfey B.A., Hamdane D. An enzymatic activation of formaldehyde for nucleotide methylation Nature Communications. 2021;12(1)
Dulchavsky M., Clark C.T., Bardwell J.C.A., Stull F. A cytochrome c is the natural electron acceptor for nicotine oxidoreductase Nature Chemical Biology. 2021;17(3):344-350.
Dulchavsky M., Clark C.T., Bardwell J.C.A., Stull F. Author Correction: A cytochrome c is the natural electron acceptor for nicotine oxidoreductase (Nature Chemical Biology, (2021), 17, 3, (344-350), 10.1038/s41589-020-00712-3) Nature Chemical Biology. 2021;17(3):360.
Matthews A., Saleem-Batcha R., Sanders J.N., Stull F., Houk K.N., Teufel R. Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases Nature Chemical Biology. 2020;16(5):556-563.
Meinen B.A., Gadkari V.V., Stull F., Ruotolo B.T., Bardwell J.C.A. SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins Proceedings of the National Academy of Sciences of the United States of America. 2019;116(46):23040-23049.
Saleem-Batcha R., Stull F., Sanders J.N., Moore B.S., Palfey B.A., Houk K.N., Teufel R. Erratum: Enzymatic control of dioxygen binding and functionalization of the flavin cofactor (Proceedings of the National Academy of Sciences of the United States of America (2018) 115 (4909-4914) DOI: 10.1073/pnas.1801189115 Proceedings of the National Academy of Sciences of the United States of America. 2019;116(30):15309.
Wu K., Stull F., Lee C., Bardwell J.C.A. Protein folding while chaperone bound is dependent on weak interactions Nature Communications. 2019;10(1)
Horowitz S., Koldewey P., Stull F., Bardwell J. Folding while bound to chaperones Current Opinion in Structural Biology. 2018;48:1-5.
Saleem-Batcha R., Stull F., Sanders J.N., Moore B.S., Palfey B.A., Houk K.N., Teufel R. Enzymatic control of dioxygen binding and functionalization of the flavin cofactor Proceedings of the National Academy of Sciences of the United States of America. 2018;115(19):4909-4919.
Salmon L., Stull F., Sayle S., Cato C., Akgül Ş., Foit L., Ahlstrom L.S., Eisenmesser E.Z., Al-Hashimi H.M., Bardwell J.C.A., Horowitz S. The Mechanism of HdeA Unfolding and Chaperone Activation Journal of Molecular Biology. 2018;430(1):33-40.
Stull F., Bardwell J. Folding against the wind news-and-views Nature Chemical Biology. 2018;14(4):329-330.
Stull F., Betton J.M., Bardwell J.C.A. Periplasmic Chaperones and Prolyl Isomerases EcoSal Plus. 2018;8(1)
Stull F., Hipp H., Stockbridge R., Bardwell J. In vivo chloride concentrations surge to proteotoxic levels during acid stress Nature Chemical Biology. 2018;14(11):1051-1058.
Koldewey P., Stull F., Horowitz S., Martin R., Bardwell J.C.A. Forces Driving Chaperone Action Cell. 2016;166(2):369-379.
Stull F., Koldewey P., Humes J., Radford S., Bardwell J. Substrate protein folds while it is bound to the ATP-independent chaperone Spy Nature Structural and Molecular Biology. 2016;23(1):53-58.
Stull F.W., Bernard S.M., Sapra A., Smith J.L., Zuiderweg E.R.P., Palfey B.A. Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase Biochemistry. 2016;55(23):3261-3269.
Teufel R., Stull F., Meehan M., Michaudel Q., Dorrestein P., Palfey B., Moore B. Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor Journal of the American Chemical Society. 2015;137(25):8078-8085.
Nikolova E., Stull F., Al-Hashimi H.M. Guanine to inosine substitution leads to large increases in the population of a transient G·C hoogsteen base pair Biochemistry. 2014;53(46):7145-7147.
Teufel R., Miyanaga A., Michaudel Q., Stull F., Louie G., Noel J., Baran P., Palfey B., Moore B. Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement Nature. 2013;503(7477):552-556.
Stull F.W., Martin D.F. Comparative ease of separation of mixtures of selected nuisance anions (nitrate, nitrite, sulfate, phosphate) using Octolig <sup>®</sup> Journal of Environmental Science and Health - Part A Toxic/Hazardous Substances and Environmental Engineering. 2009;44(14):1545-1550.
Martin D.F., Aguinaldo J.S., Kondis N.P., Stull F.W., O'Donnell L.F., Martin B.B., Alldredge R.L. Comparison of effectiveness of removal of nuisance anions by metalloligs, metal derivatives of Octolig® Journal of Environmental Science and Health - Part A Toxic/Hazardous Substances and Environmental Engineering. 2008;43(11):1296-1302.