CV Lattes
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Universidade de São Paulo (USP). Instituto de Química (IQ) (Institutional affiliation for the last research proposal) Birthplace: Brazil
holds a Bachelor in Chemistry (1999), Ph.D. in Biochemistry (2004) and a Habilitation (2016), obtained at the Institute of Chemistry at the University of São Paulo (IQ-USP). He was a postdoctoral fellow at the Department of Chemistry at the University of Warwick, UK (2005) and at the Department of Fundamental Chemistry at IQ-USP (2006-2007). Currently, he is an Associate Professor at the Biochemistry Department of USP. He has experience in Physical Chemistry, Biophysics and Biochemistry, with emphasis on the calculation and development of methods in electronic structure, computational enzymology and simulation with potential hybrid (QM/MM), molecular dynamics of proteins and estimation of free energies. (Source: Lattes Curriculum)
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Electron transport chain enzymes in mitochondria and bacteria are equipped with transition metal-based prosthetic groups involved in essential oxidoreduction processes. In this project we propose to elucidate catalytic mechanisms and the structural stability of metal cofactors bound in these proteins. We will investigate the mechanisms of proton-electron coupled transfer (PCET) reactions …
We seek funds to help propose and establish a long-term collaboration in both computational bioinorganic chemistry and in high-end computing and its applications in computational science. The authors have collaborated in the past on the former topic, including a peer-reviewed publication. The current activities and future plans of the Health Science Platform at Tianjin University and the…
Computer simulation has increasing presence and importance for research in chemistry, biochemistry and molecular biophysics. A clear recognition of this research area was the Nobel prize in Chemistry awarded in 2013 for the development of hybrid methods in molecular simulation.The research proposal presented here will be conducted in the Computational Biochemistry and Biophysics laborator…
There is an increasing importance of computer simulation in the areas of chemistry, biochemistry and molecular biophysics. The Nobel Prize in Chemistry awarded in 2013 for the development of hybrid methods of molecular simulation is a clear recognition of this importance.The research proposal presented here will be carried out in the Computational Biochemistry and Biophysics laboratory re…
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Respiratory complex I transduces about half of the chemical energy used in a cell by catalyzing the transfer of electrons from the NADH metabolite to coenzyme-Q coupled to proton pumping and the generation of a transmembrane electrochemical gradient. Although decades of research, including impressive recent structural advances, have contributed to unveil the molecular functioning of compl…
The coenzyme Q: cytochrome C oxidoreductase, or respiratory complex III, catalyzes the oxidoreduction of quinols and quinones (coenzyme Q or simply Q) substrates coupled to membrane translocation of protons, in the so-called modified Q-cycle. The study of the mechanism of action of this protein complex, which is fundamental to cellular respiration and photosynthesis (by the homologous cyt…
Respiratory complex II couples succinate oxidation to quinone reduction in the electron transport chain. In succinate oxidation, a FAD molecule is reduced and, then, electrons are passed through three iron-sulfur clusters to reduce a quinone. The mechanism of succinate oxidation to fumarate has been the subject of study in the candidate masters degree. Here, we propose to extend the compl…
(Only some records are available in English at this moment)
Iron-sulfur clusters (FeS) are the most abundant metal cofactors involved in biological redox reactions. Their electronic structure with multiple low-lying and near-degenerate states is very difficult to model accurately. But, the advent of advanced electronic structure methods such as density matrix renormalization group (DMRG) and selected configuration interaction (sCI) have opened the…
The T4 lysozyme L99A mutant is a protein often used to study small molecule binding to macromolecules. Crystal structures of the L99A mutant complexed with ligands show that the opening on the protein surface for ligand entry and scape from the engineered binding site is small. Thus, the protein must have a "conformational breath" to allow ligand excursion to the binding site. However, th…
| 2 / 2 | Ongoing research grants |
| 8 / 6 | Completed research grants |
| 1 / 1 | Ongoing scholarships in Brazil |
| 12 / 8 | Completed scholarships in Brazil |
| 2 / 2 | Completed scholarships abroad |
| 25 / 19 | All research grants and scholarships |
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