Event Title
Conformational Sampling of Glucose Oxidase for Bio-fuel Cell Applications
Faculty Sponsor
Dhruva Chakravorty
Submission Type
Poster
Description
Glucose Oxidase (GOX) is a redox enzyme that uses flavin adenine dinucleotide (FAD) as a cofactor to reduce β-D-glucose into δ-gluconolactone via a ping-pong steady-state kinetic mechanism. While it remains a candidate for developing alternative fuel cells, instability of the dimeric interface remains a concern. Electrochemistry experiments have determined that enzymatic efficiency depends upon the orientation of FAD to a carbon nanotube. Our hypothesis is that the orientation of FAD effects the conformational space sampled by the protein. Towards this we have applied computational chemistry methods to identify the way in which glycolysation reaction impacts the various oligomeric states of GOX. In close agreement with literature, molecular dynamics simulations of apo-GOX find that the protein undergoes large conformational changes that have been implicated in the modulating the glycosylation reaction. Our long-term goal is to develop computational chemistry methods in order to simulate the entire protein and electrode assembly in order to provide a means to stabilize GOX for applications in a bio-battery.
Conformational Sampling of Glucose Oxidase for Bio-fuel Cell Applications
Glucose Oxidase (GOX) is a redox enzyme that uses flavin adenine dinucleotide (FAD) as a cofactor to reduce β-D-glucose into δ-gluconolactone via a ping-pong steady-state kinetic mechanism. While it remains a candidate for developing alternative fuel cells, instability of the dimeric interface remains a concern. Electrochemistry experiments have determined that enzymatic efficiency depends upon the orientation of FAD to a carbon nanotube. Our hypothesis is that the orientation of FAD effects the conformational space sampled by the protein. Towards this we have applied computational chemistry methods to identify the way in which glycolysation reaction impacts the various oligomeric states of GOX. In close agreement with literature, molecular dynamics simulations of apo-GOX find that the protein undergoes large conformational changes that have been implicated in the modulating the glycosylation reaction. Our long-term goal is to develop computational chemistry methods in order to simulate the entire protein and electrode assembly in order to provide a means to stabilize GOX for applications in a bio-battery.
Comments
1st place, Poster