Development of nanostructured metal surfaces for application in surface intensifie...
| 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. | |