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Sydney Johnson

Biochemistry Ph.D. Candidate
  • Research area(s): Flavin-dependent monooxygenases, natural product biosynthesis, and xenobiotic detoxification
Sydney Johnson
107 Fralin Hall
  • Lab Phone: (540) 231-0084

Ph.D., Biochemistry, Virginia Tech, 2024 Expected

B.S., Biochemistry and Molecular and Cellular Biology, University of New Hampshire, 2018

Sobrado Lab, Virginia Tech, Blacksburg, VA, December 2019-present

Research Associate I, Matrivax Research and Development, Boston, MA, May 2018-July 2019

Virginia Tech Biochemistry Teaching Award, 2022

Virginia Tech Center for Drug Discovery Conference, Best Presentation, 2022

Biochemistry Graduate Student Association Mentoring Fellowship Recipient, Virginia Tech, 2022

Graduate Student Research and Professional Development Grant, Virginia Tech, 2021

Instructor of Record for BCHM 4115: General Biochemistry 5/2022-12/2022

Graduate Teaching Scholars Program Member 9/2021-present

Teaching Assistant for BCHM 2024: Concepts of Biochemistry 9/2020-12/2020

Teaching Assistant for BCHM 4115: General Biochemistry 9/2019-12/2019

Program Focus

My research is focused on solving the kinetic and chemical mechanism of unique flavin-dependent monooxygenases (FMOs). The FMO family is a large and diverse group of enzymes that have biological roles ranging from various catabolic processes to light emission. My projects particularly focus on novel FMOs involved in natural product biosynthesis and insect xenobiotic detoxification.

Each of the enzymes I study carries out chemistry rarely seen by FMOs such as multiple iterative oxidation reactions or the oxidation of tertiary amines. I have worked to develop several assays to study their unique product formation and iterative oxidation functionality by utilizing a combination of oxygen consumption, HPLC, mass spectrometry, and colorimetric assays. Since FMOs carry out redox chemistry, their catalysis can be split up into two parts: the reductive and oxidative-half reactions.

I have been able to study these by conducting rapid-rate kinetics using a stopped-flow spectrophotometer in an anaerobic chamber. The overarching goal of this work is to utilize these solved mechanisms to engineer the enzymes in such a way that will expand their substrate scope for biomedical application.

Further, we aim to inhibit the insect FMOs that are involved in detoxifying xenobiotics such as insecticides to aid the global agricultural industry in the successful growing of crops that they eat. 

Oral Presentations

  • 2022 Biochemistry Spring Seminar Series, Virginia Tech
    • Presentation Title: Biochemical Characterization of Unique Flavin-Dependent Monooxygenases Involved in Natural Product Biosynthesis
  • 2021 Midwest Enzyme Chemistry Conference, Grand Valley State University
    • Presentation Title: Biochemical Characterization of OxaD, a Nitrone Forming Flavin-Dependent Monooxygenase
  • 2021 Southeast Enzyme Conference, Georgia State University (virtual)
    • Presentation Title: Kinetic Characterization of the Novel N-Monooxygenase, CreE, involved in Nitro Functional Group Formation
  • 2021 Virginia Academy of Science Spring Meeting (virtual)
    • Presentation Title: Biochemical Characterization of a Flavin-Dependent Monooxygenase from the Insect Pest, Zonocerus variegatus
  • 2020 Graduate Student Association Research Symposium, Virginia Tech
    • Presentation Title: Performing Challenging Reactions with Enzymes: The Formation of Diazo Groups by CreE

Poster Presentations

  • 2022 Southeast Enzyme Conference, Georgia State University
    • Presentation Title: Biochemical Characterization of a Flavin-Dependent Monooxygenase from the Insect Pest, Zonocerus variegatus
  • 2022 Virginia Tech Center for Drug Discovery Conference, Virginia Tech
    • Presentation Title: Biochemical Characterization of a Flavin-Dependent Monooxygenase from the Insect Pest, Zonocerus variegatus
  • 2022 Enzyme Mechanism Conference, Loews Ventana Canyon, Tucson AZ
    • Presentation Title: Structural and Kinetic Characterization of a Nitro-Forming Flavin-Dependent Monooxygenase, CreE