Profile
Isabel Moura received her Degree in Chemical Engineering from Technical University of Lisbon (Pt) in 1974. Received a master degree in Physical Inorganic Chemistry in 1977 and the PhD from New University of Lisbon (NOVA) in 1981. Assistant Professor until 1981 and 1986 became Associate Professor at Department of Chemistry, School of Sciences and Technology, NOVA, Campus of Caparica (Pt), got the habilitation in 1994 and became a Full Professor in 1997 at NOVA. During her career was Visiting Professor in University of Georgia, Athens, USA. During the period 2000/2011, Head of the Chemistry Department of FCT/UNL and Director of the Associated Laboratory REQUIMTE for Sustainable Chemistry. 34 PhD Thesis were oriented and 30 Science Projects as Principal Investigator.
The main work is centered on the Structure-Function of Metalloproteins. Application of biochemical and spectroscopic tools (NMR, EPR and Mössbauer). Proteins involved in relevant bacterial metabolic pathways – N and S Biocycles. Active sites include Cu, Co, hemes, iron-sulfur centers (rubredoxin type, [2Fe-4S], [3Fe-4S], [4Fe-4S]) as well as association of Fe-S centers with Mo, W, Ni, siroheme and flavines. New type of clusters and new metal associations is also one of the main topics of research. Recently a major emphasis has been the study of enzymes from the denitrification pathway mainly nitrous oxide reductase a copper enzyme with an unusual copper center (the catalytic site) with four copper atoms and nitric oxide reductase (a membrane enzyme) with a binuclear iron center as the catalytic center. Both these enzymes catalyse the two last steps of the denitrification pathway.
In respect to nitrous oxide reductase the last enzyme of the denitrification pathway the main achievement was the discovery of a new type of copper cluster containing four copper atoms and a sulfur in the middle (CuZ). My group has been involved in understanding he mechanism of activation revealing two forms of the copper cluster. The catalytic mechanism of the enzyme was explored showing that a completely reduced form of the cluster is needed to catalyze N2O and a new catalytic intermediate was identified (CuZº). A proton/electron couple mechanism was also proposed based on potentiometric and electrochemical studies. Nitric oxide reductase a membrane enzyme has been fully characterized, and several attempts were made to construct a NO biosensor.
Another enzyme that was well studied is the dissimilatory nitrite reductase that reduces nitrite to ammonia. The enzyme contains five c-type hemes in one of the subunities NirA. EPR and Mossbauer was very important in revealing that one of the hemes in the largest subunitie is high spin and the catalytic site of the enzyme. This enzyme is quite versatile being able depending on the state of reduction to reduce nitrite to ammonia or NO to N2O.
She is member of the Academy of Sciences Portugal (2020), European Academy of Sciences (2021), Portuguese Chemical Society, Biochemistry Portuguese Society and Society of Biological Inorganic Chemistry, panel of Evaluation of Advanced ERC Grants (since 2016) and integrates the Editorial Board of Journal Inorganic Biochemistry and Journal of Biological Inorganic Chemistry.
She received distinctions and awards: Prize Alberto Romão Dias (2024), Ministry of Sciences and Technology (MCTES) (2005), Portugal-France Association (APDF) (2002) Marquês de Pombal Foundation (1995) and was nominated as a Women in Science by Ciência Viva.
