Title of Oral/Poster Presentation

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

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Apr 9th, 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.