The photoprotection of Flavin Adenine Dinucleotide and Riboflavin by 5,10-methenyltetrahydrofolate
Presentation Type
Abstract
Faculty Advisor
Johannes Schelvis
Access Type
Event
Start Date
25-4-2025 10:30 AM
End Date
25-4-2025 11:29 AM
Description
Flavin adenine dinucleotide (FAD) and 5,10-methyltetrahydrofolate (MTHF) are two essential molecules present in enzymes and proteins that harness light for DNA repair, as well as for signaling in plant growth and the regulation of circadian rhythms in animals. This research explores the hypothesis that MTHF offers protective advantages to FAD under conditions of an elevated light intensity. This hypothesis is examined through experimental procedures involving the two molecules in solution, followed by comprehensive analysis within the context of enzymatic and protein functions. The potential protection of FAD by MTHF is significant, considering its classification as a vital cofactor in numerous enzymatic and protein activities. The effects of irradiation on of FAD, both in the presence and absence of MTHF, will be investigated utilising various advanced methodologies, including absorption spectroscopy, liquid chromatography (LC), and LC-mass spectrometry, to clarify the reaction intermediates and products to develop a better understanding of how MTHF protects FAD. In addition, riboflavin or vitamin B2 is studied to determine the effect of MTHF on its stability. Riboflavin is an essential vitamin and plays an important role within the food industry. Riboflavin is prevalent in numerous products available on store shelves, and its stability during storage is of great importance. In summary, this study aims to better understand the role of MTHF in protecting FAD in critical enzymes as well as its potential in stabilizing riboflavin in consumer products.
The photoprotection of Flavin Adenine Dinucleotide and Riboflavin by 5,10-methenyltetrahydrofolate
Flavin adenine dinucleotide (FAD) and 5,10-methyltetrahydrofolate (MTHF) are two essential molecules present in enzymes and proteins that harness light for DNA repair, as well as for signaling in plant growth and the regulation of circadian rhythms in animals. This research explores the hypothesis that MTHF offers protective advantages to FAD under conditions of an elevated light intensity. This hypothesis is examined through experimental procedures involving the two molecules in solution, followed by comprehensive analysis within the context of enzymatic and protein functions. The potential protection of FAD by MTHF is significant, considering its classification as a vital cofactor in numerous enzymatic and protein activities. The effects of irradiation on of FAD, both in the presence and absence of MTHF, will be investigated utilising various advanced methodologies, including absorption spectroscopy, liquid chromatography (LC), and LC-mass spectrometry, to clarify the reaction intermediates and products to develop a better understanding of how MTHF protects FAD. In addition, riboflavin or vitamin B2 is studied to determine the effect of MTHF on its stability. Riboflavin is an essential vitamin and plays an important role within the food industry. Riboflavin is prevalent in numerous products available on store shelves, and its stability during storage is of great importance. In summary, this study aims to better understand the role of MTHF in protecting FAD in critical enzymes as well as its potential in stabilizing riboflavin in consumer products.
Comments
Poster presentation at the 2025 Student Research Symposium.