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Keri Colabroy - Muhlenberg College. Allentown, PA, UNITED STATES

Keri Colabroy

Associate Professor of Chemistry | Muhlenberg College

Allentown, PA, UNITED STATES

Dr. Keri Colabroy's research interest is the chemistry of biological, particularly mechanisms used by enzymes to catalyze complex reactions.

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Biography

Dr. Keri Colabroy's primary research interest is the chemistry of biological systems. She is fascinated by the mechanisms used by enzymes to catalyze complex reactions. Enzymes catalyze specific transformations in aqueous solution and at ambient temperature that would not be possible using techniques of organic chemistry. Her PhD work focused on understanding the mechanism by which 3-hydroxyanthraniliate is converted using enzymatic and non-enzymatic steps to quiniolinic acid, a precursor to the redox cofactor nicotinamide adenine dinucleotide. Secondary metabolites such as antibiotics are often complicated structures that involve multiple interesting enzymatic steps to assemble. Her present work includes using the tools of chemistry to understand the enzymatic mechanisms of antibiotic assembly. Research interests are in the chemistry of biological systems, specifically in the area of mechanistic enzymology with a focus on antibiotic biosynthesis. This work uses a variety of techniques drawn from different fields including molecular biology, organic chemistry and classical biochemistry, to elucidate enzyme mechanism and function.

Areas of Expertise (7)

Organic Chemistry

Biochemistry

Classical Biochemistry

Molecular Biology

Chemistry of Biologiccal Systems

Enzyme Mechanisms

Enzyme Functions

Education (3)

Cornell University: Ph.D.

Cornell University: M.S.

Messiah College: B.S.

Media Appearances (2)

Muhlenberg's Keri Colabroy blends food and science

The Allentown Morning Call  print

2016-06-28

Keri Colabroy whisked the molten syrup in a saucepan in a Muhlenberg College classroom The South Whitehall Township woman was making soft caramels using simple ingredients — cream, butter, sugar, corn syrup and water (and a bit of salt and vanilla). This was no ordinary candy-making demonstration. "That buttery, toasty smell of caramel are the molecules traveling up your nose," says the associate professor of chemistry and co-director of the biochemistry program at Allentown's Muhlenberg College. Colabroy was demonstrating how a simple caramel is the result of a complex series of chemical (and tasty) reactions ...

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Smart food: Cook better with a little science

The Inquirer Daily News  print

2016-11-10

On Muhlenberg College's campus in Allentown, some students are learning to make caramel, not in a culinary program, but in a science class. Keri Colabroy, an associate professor of chemistry and biology, has been offering "The Science of Cooking" since 2012, with the lab portion convening in the kitchen. There, the students learn the molecular composition of different fats, the chemical reasons eggs harden as they cook, and how the protein content in flour affects the bread you bake with it. Now, she's written a textbook, The Science of Cooking, to make science more palatable for students who fear chemistry and biology. "Chemistry is learnable by anybody, but when we present it the way we usually do in an academic environment, it's abstract," says Colabroy. "It's like trying to teach a child to write in a language they don't speak" ...

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Articles (3)

Tearing Down to Build Up: Metalloenzymes in the Biosynthesis Lincomycin, Hormaomycin and the Pyrrolo


Biochimica Et Biophysica Acta

2016

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A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin


Biochemistry

2011 We report the first characterization and classification of Orf13 (S. refuineus) as a heme-dependent peroxidase catalyzing the ortho-hydroxylation of l-tyrosine to l-DOPA. The putative tyrosine hydroxylase coded by orf13 of the anthramycin biosynthesis gene cluster has been expressed and purified. Heme b has been identified as the required cofactor for catalysis, and maximal l-tyrosine conversion to l-DOPA is observed in the presence of hydrogen peroxide. Preincubation of l-tyrosine with Orf13 prior to the addition of hydrogen peroxide is required for l-DOPA production. However, the enzyme becomes inactivated by hydrogen peroxide during catalysis. Steady-state kinetic analysis of l-tyrosine hydroxylation revealed similar catalytic efficiency for both l-tyrosine and hydrogen peroxide. Spectroscopic data from a reduced-CO(g) UV–vis spectrum of Orf13 and electron paramagnetic resonance of ferric heme Orf13 are consistent with heme peroxidases that have a histidyl-ligated heme iron. Contrary to the classical heme peroxidase oxidation reaction with hydrogen peroxide that produces coupled aromatic products such as o,o′-dityrosine, Orf13 is novel in its ability to catalyze aromatic amino acid hydroxylation with hydrogen peroxide, in the substrate addition order and for its substrate specificity for l-tyrosine. Peroxygenase activity of Orf13 for the ortho-hydroxylation of l-tyrosine to l-DOPA by a molecular oxygen dependent pathway in the presence of dihydroxyfumaric acid is also observed. This reaction behavior is consistent with peroxygenase activity reported with horseradish peroxidase for the hydroxylation of phenol. Overall, the putative function of Orf13 as a tyrosine hydroxylase has been confirmed and establishes the first bacterial class of tyrosine hydroxylases.

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A writing-intensive, methods-based laboratory course for undergraduates


Biochemistry and Molecular Biology Education

2011 Engaging undergraduate students in designing and executing original research should not only be accompanied by technique training but also intentional instruction in the critical analysis and writing of scientific literature. The course described here takes a rigorous approach to scientific reading and writing using primary literature as the model while simultaneously integrating laboratory instruction on basic enzyme purification and characterization, followed by 6 weeks of laboratory dedicated to student-designed original research projects. In the preparation and execution of their original projects, students engage in analysis of the primary literature, proposal writing, peer review, manuscript preparation, and oral presentation. The result is a comprehensive and challenging course that teaches third- and fourth-year undergraduates what it means to “think and work like a scientist.”

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