I obtained a Biochemistry degree in 1998 at Faculdade de Ciências, Porto University. Afterward, I started a PhD in Chemistry at the same institution focusing on the enzymatic mechanisms of firefly luciferase. This PhD resulted from a collaboration between Departamento de Química da Faculdade de Ciências and Serviço de Bioquímica da Faculdade de Medicina da Universidade do Porto. During my PhD I was able to explain why coenzyme A, used as an additive in commercial cocktails, was able to stimulate the luminescence reaction. Throughout my PhD I also worked as a "Monitor" at the Serviço de Bioquímica da Faculdade de Medicina. I was lecturer for "Laboratórios de Bioquímica" in the classes of 2003/04, 2004/05 and 2005/06. After my PhD, I joined the laboratory of Prof Woodland Hastings at Molecular Cellular Biology (MCB), Harvard University, USA, where I pursued studies on bioluminescence. In 2008, after Prof. Hastings jubilation, I transferred to the lab of Prof. Alfred Goldberg at the Department of Cell Biology at Harvard Medical School. At the Goldberg Lab I was able to propose a mechanism for the functioning of the AAA+ hexameric ring PAN, a 19S proteasome homologue, and show that although PAN has six identical subunits it binds ATPs in pairs, and its subunits exhibit three conformational states with high, low, or no affinity for ATP. In 2009 I returned to Portugal and initialized studies with a small protein isolated from the parasite Fasciola hepatica (FH8). Sequence analysis revealed that FH8 had two EF-hand Ca2+-binding motifs. I showed that the protein binds Ca2+, promoting large conformational changes, and behaves like a Ca2+ sensor. In 2011, I relocated to Salvador Ventura Lab and I was able to demonstrate that Tim15, involved in the chaperoning of mtHsp70 in the mitochondrial matrix, shifts from an essentially unfolded peptide to a folded peptide upon Zn2+ coordination. Moreover, I established unambiguously that Tim15 folding is essential for its role as mtHsp70 chaperone. I also studied the oxidative folding of Cox19, a small twin CX9C motif protein, involved in the copper efflux to the mitochondrial Intermembrane space. I demonstrated that Cox19 when fully reduced is unfolded but when imported into the IMS, it rapidly folds as a consequence of its oxidation catalyzed by Mia40. Mia40s role is to funnel a rough folding landscape, skipping the accumulation of kinetic traps. In 2014, I moved to the Boisbouvier lab, Institut de Biologie Strucuturale, Grenoble, France, where I initialized studies on ClpP, a bacterial protease also present in mitochondria and an important drug target. In the same year, I was invited by Prof Alfred Golberg, Harvard Medical School, to optimize HTS assays at Glaxo Smith and Kline Open Lab aimed at the discovery of inhibitors for the ClpCP1P2 complex from Mtb. A collaboration project involving Institut de Biologie Strucuturale, Harvard Medical School and Glaxo Smith and Kline was initiated. I am last corresponding author in the 3 publications derived from this project (articles 1,3 and 4). Since 2019 I am an independent researcher at Faculdade de Medicina da Universidade do Porto/i3S Porto, Portugal. During my research career, I published 28 articles in peer-reviewed journals, including journals as Cell, Science Advances, Nature Communications and Angewandte Chemie, with a total of more than 1100 citations (google scholar, h-index 17). 17 were published as first author and 9 were published as corresponding author. I was also involved in the supervision of two master students and as described above worked as a lecturer at the Faculdade de Medicina da Universidade do Porto.