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Investigating the Stoichiometry of RuBisCO Activase by Fluorescence Fluctuation Spectroscopy

Abstract Ribulose-1, 5-bisphosphate carboxylase oxygenase, commonly known as RuBisCO, is an enzyme involved in carbon fixation in photosynthetic organisms. The enzyme is subject to a mechanism-based deactivation during its catalytic cycle. RuBisCO activase (Rca), an ancillary enzyme belonging to the AAA+ family of the ATP-ases, rescues RuBisCO by facilitating the removal of the tightly bound sugar phosphates from the active sites of RuBisCO. In this work, we investigated the ATP/ADP dependent oligomerization equilibrium of fluorescently tagged Rca for a wide range of concentrations using fluorescence correlation spectroscopy. Results show that in the presence of ADP-Mg2+, the oligomerization state of Rca gradually changes in steps of two subunits. T... (more)
Created Date 2014
Contributor Chakraborty, Manas (Author) / Levitus, Marcia (Advisor) / Angell, Charles (Committee member) / Lindsay, Stuart (Committee member) / Arizona State University (Publisher)
Subject Chemistry / Biophysics / FCS / PCH / Protein oligomerization / Rubisco Activase
Type Doctoral Dissertation
Extent 132 pages
Language English
Reuse Permissions All Rights Reserved
Note Ph.D. Chemistry 2014
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS

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Description Dissertation/Thesis