The role of dual-ATP motors in substrate reduction by DPOR
Class
Article
Department
Chemistry and Biochemistry
Faculty Mentor
Edwin Antony
Presentation Type
Poster Presentation
Abstract
Dark-operative protochlorophyllide reductase (DPOR) is a nitrogenase-like protein that catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide). This reaction is the penultimate step in the biosynthesis of the pigment chlorophyll, which is fundamental to the process of photosynthesis. The structure of DPOR resembles that of nitrogenase, but varies in the composition of the metal clusters associated within its active sites. Both DPOR and nitrogenase have four ATP binding sites - two per side, and these binding sites are located within the L-protein. This project's goal is to generate a half-reactive DPOR, in which half of the L-dimer is rendered inert to ATP binding and hydrolysis. To achieve this objective, we have created a genetically linked-L-protein dimer, giving us the ability to render one, or both, L proteins inert. Knocking out selected ATP binding sites allows us to determine the kinetics of ATP reactions within DPOR's L-dimer structure, such as determining the necessity of both ATP molecules binding on one side of the DPOR complex.
Start Date
4-9-2015 3:00 PM
The role of dual-ATP motors in substrate reduction by DPOR
Dark-operative protochlorophyllide reductase (DPOR) is a nitrogenase-like protein that catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide). This reaction is the penultimate step in the biosynthesis of the pigment chlorophyll, which is fundamental to the process of photosynthesis. The structure of DPOR resembles that of nitrogenase, but varies in the composition of the metal clusters associated within its active sites. Both DPOR and nitrogenase have four ATP binding sites - two per side, and these binding sites are located within the L-protein. This project's goal is to generate a half-reactive DPOR, in which half of the L-dimer is rendered inert to ATP binding and hydrolysis. To achieve this objective, we have created a genetically linked-L-protein dimer, giving us the ability to render one, or both, L proteins inert. Knocking out selected ATP binding sites allows us to determine the kinetics of ATP reactions within DPOR's L-dimer structure, such as determining the necessity of both ATP molecules binding on one side of the DPOR complex.