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. 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.