Exploiting new facets of the interaction between chlorocatechol 1,2-dioxygenase and its ligands

• Grant number: 12/19595-1
• Support Opportunities: Scholarships in Brazil - Master
• Start date: December 01, 2012
• End date: January 31, 2014
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Antonio José da Costa Filho
• Grantee: Natasha Faiani Furtado
• Host Institution: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil

Abstract

The use of chlorinated compounds bearing aromatic structures in their chemical composition has quickly grown in the last few years due to their general presence in processes of modern industry. The degradation of such compounds is slow, due to their high chemical stability, thus making them frequent polutants of the environment. Different strategies to tackle this problem are available. The so-called bioremediation methods are among those strategies and have been gaining many applications because of their higher efficiency and due to the use of enzymes, which do not affect the environment at all, to perform the degradation task. Chlorocatechol 1,2-dioxygenase from P. putida (Pp 1,2-CCD) is one of those enzymes and is the object of study of this proposal. Our group has been working in the understanding the mechanism of action of Pp 1,2-CCD since we believe that to achieve a more efficient use of Pp 1,2-CCD necessarily needs knowledge about ways of controlling the enzymatic activity. In this project, we seek to investigate the role of some Pp 1,2-CCD ligands in the enzyme reaction. In particular, we intend to identify the anfiphatic molecules present in the enzyme structure. After that it is our goal to work on methods to remove those molecules, which will allow us to study their influence on catalysis. This part of the study will also include investigations of the potential interaction between the enzyme and membrane models. Furthermore, it is our interest to perform kinetic studies of Pp 1,2-CCD towards its ideal substrate, chlorocatechol, and look for inhibition/modulation mechanism of the enzyme catalysis.

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

FURTADO, Natasha Faiani. Exploring new facets of the interaction between the enzyme chlorocatechol 1,2-dioxygenase and its ligands. 2014. Master's Dissertation - Universidade de São Paulo (USP). Faculdade de Ciências Farmacêuticas de Ribeirão Preto (PCARP/BC) Ribeirão Preto.