The primary carbon fixing enzyme Rubisco maintains its activity through release of trapped inhibitors by Rubisco activase (Rca). Very little is known about the interaction, but binding has been proposed to be weak and transient. Extensive effort was made to develop Förster resonance energy transfer (FRET) based assays to understand the physical interaction between Rubisco and Rca, as well as understand subunit exchange in Rca.
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- Partial requirement for: Ph.D., Arizona State University, 2017Note typethesis
- Includes bibliographical references (pages 111-121)Note typebibliography
- Field of study: Biochemistry