Submission Type
Poster
Start Date
April 2020
Abstract
Because of humans’ heavy impact on nature with industrialization and resource extraction, biomimetics, also known as biomimicry, is a study that has emerged. Biomimetics utilizes observations from nature to comprehend the principles of underlying mechanisms and apply concepts that may benefit science, medicine, engineering and the like. An area of biochemistry we are applying this to is the lactate racemase enzyme.This metalloenzyme is found in many prokaryotic organisms and catalyzes the interconversion between the two optical isomers of lactic acid. The structure of this enzyme consists of a square-planar nickel (II) ion coordinated by a histidine residue and a pincer ligand. We are synthesizing a model of this enzyme using biomimetic chemistry to further expand our knowledge on the mechanism and reactivity of lactate racemase. We hope that the findings from this model will lead to a greater understanding of the unique organometallic cofactor of lactate racemase. This will help improve designs for biomimetic catalysts that can be used in many different areas of everyday life, especially but not exclusively, renewable fuels.
Recommended Citation
Podguski, Stephanie and Ross, Maisy, "295— Biomimicry: Investigating the Active Site Model of Lactate Racemase" (2020). GREAT Day Posters. 23.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2020/posters-2020/23
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License
Included in
Biochemistry Commons, Inorganic Chemistry Commons, Other Chemistry Commons, Other Environmental Sciences Commons, Sustainability Commons
295— Biomimicry: Investigating the Active Site Model of Lactate Racemase
Because of humans’ heavy impact on nature with industrialization and resource extraction, biomimetics, also known as biomimicry, is a study that has emerged. Biomimetics utilizes observations from nature to comprehend the principles of underlying mechanisms and apply concepts that may benefit science, medicine, engineering and the like. An area of biochemistry we are applying this to is the lactate racemase enzyme.This metalloenzyme is found in many prokaryotic organisms and catalyzes the interconversion between the two optical isomers of lactic acid. The structure of this enzyme consists of a square-planar nickel (II) ion coordinated by a histidine residue and a pincer ligand. We are synthesizing a model of this enzyme using biomimetic chemistry to further expand our knowledge on the mechanism and reactivity of lactate racemase. We hope that the findings from this model will lead to a greater understanding of the unique organometallic cofactor of lactate racemase. This will help improve designs for biomimetic catalysts that can be used in many different areas of everyday life, especially but not exclusively, renewable fuels.
Comments
Advisor: Dr. Brandon Tate