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Study of metalloenzymes through electrochemistry coupled to vibrational spectroscopy

Grant number: 17/20493-2
Support type:Scholarships in Brazil - Doctorate
Effective date (Start): February 01, 2018
Effective date (End): January 31, 2021
Field of knowledge:Physical Sciences and Mathematics - Chemistry
Principal Investigator:Frank Nelson Crespilho
Grantee:Lucyano Jefferson Alves de Macêdo
Home Institution: Instituto de Química de São Carlos (IQSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:13/14262-7 - Nanostructured films from biologically-relevant materials, AP.TEM

Abstract

Among the different types of proteins, enzymes are those whose main function is the catalysis in biological medium. The class known as metalloenzymes is represented by the enzymes whose structure has a prosthetic group containing one or more metallic atoms, which often are coordinated to organometallic unities. For many years, it was presumed that those prosthetic groups performed a role only in terms of structure, that is, they kept the three-dimensional structure of the enzyme and, consequently, their functionality and catalytic efficiency. However, recent studies point out that, for metalloenzymes, prosthetic groups perform roles far beyond the structural, interfering, for example, on the electron transfer, communication between the active site and the substrate and signalizing of molecular events. Therefore, this PhD project proposes the study of metallic centers of two enzymes of huge relevance in technology and biology: alcohol dehydrogenase (ADH) and endonuclease III (EndoIII). It is intended to gather electrochemical and spectroscopic information, by vibrational spectroscopy (FTIR) under electrochemical control of the redox processes of the metalloprotein. Besides, it is glimpsed the understanding of the organometallic bonds role on the catalytic performance of these enzymes. In particular for EndoIII, it is intended to study the metallic cluster [Fe4S4], given the charge transfer once the enzyme is bonded to DNA, aiming to clarify the explanation of charge transport mechanisms through the DNA double-helix.

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
MELO, ANTONIO F. A. A.; HASSAN, AYAZ; MACEDO, LUCYANO J. A.; OSICA, IZABELA; SHRESTHA, LOK KUMAR; JI, QINGMIN; OLIVEIRA, JR., OSVALDO N.; HENZIE, JOEL; ARIGA, KATSUHIKO; CRESPILHO, FRANK N. Microwires of Au-Ag Nanocages Patterned via Magnetic Nanoadhesives for Investigating Proteins using Surface Enhanced Infrared Absorption Spectroscopy. ACS APPLIED MATERIALS & INTERFACES, v. 11, n. 20, p. 18053-18061, MAY 22 2019. Web of Science Citations: 1.
MACEDO, LUCYANO J. A.; IOST, RODRIGO M.; HASSAN, AYAZ; BALASUBRAMANIAN, KANNAN; CRESPILHO, FRANK N. Bioelectronics and Interfaces Using Monolayer Graphene. CHEMELECTROCHEM, v. 6, n. 1, SI, p. 31-59, JAN 2 2019. Web of Science Citations: 3.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.