Luis Rubio is one of the world leaders in the study of nitrogenase biosynthesis and biochemistry. Protein nitrogenase catalyzes the conversion of atmospheric N2 to NH3, a process of enormous economic and environmental importance known as biological nitrogen fixation. His research group at the Center for Plant Biotechnology and Genomics (CBGP) combines molecular microbiology and anaerobic biochemistry knowledge and skills with a passion for solving complex scientific problems.
Luis Rubio’s scientific career has focused on the study and applications of molybdoenzymes. During his doctoral thesis he carried out the most exhaustive genetic-biochemical characterization to date of an assimilatory nitrate reductase. During his postdoctoral work he generated a biological tool that made it possible to stabilize the iron-molybdenum cofactor (FeMo-co) of nitrogenase, as well as some of its biosynthetic intermediates. He directed the investigation of a leading laboratory in the study of this cofactor located in the active center of nitrogenase and essential for its activity. In this period he and his group of researchers managed to purify all the proteins required for the biosynthesis of FeMo-co. Finally, they achieved the complete synthesis of FeMo-co, which was a pioneering contribution to the possibility of transferring the ability to fix N2 to economically important organisms, such as cereals. Many of his works were published in PNAS and other high impact journals. After receiving a European Starting Grant in 2008, they moved to Madrid and in August 2012 he won the position of University Professor at UPM. In 2023 he became part of the Spanish National Research Council (CSIC).
Luis Rubio’s laboratory aim to reconstitute the nitrogenase biosynthetic pathway, delivering concepts, knowledge, tools and methodologies for engineering nitrogen fixation in staple cereal crops. Synthetic biology, plant and yeast cell cultures, combinatorial genetic transformation of cereals and model plants, and biochemical complementation assays of resulting nitrogen fixation proteins are the tools being used. In addition, his group tries to understand the unique reactions taking place in the biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase. Finally, they contribute knowledge and technology to the other widely recognized biotechnological application of nitrogenase, which is the biological production of H2, a clean energy vector.
Currently, his laboratory carries out three lines of research with the following objectives:
ACS Synth. Biol. 2022, 11, 9, 3028–3036
2022 | Journal article
DOI: 10.1021/acssynbio.2c00194
CONTRIBUTORS: Wenshu He, Stefan Burén, Can Baysal, Xi Jiang, Teresa Capell, Paul Christou, and Luis M. Rubio
mBio. 2022 Jun 28;13(3):e0026822
2022 | Journal article
DOI: 10.1128/mbio.00268-22
CONTRIBUTORS: Xi Jiang; Diana Coroian; Emma Barahona; Carlos Echavarri-Erasun; Rocío Castellanos-Rueda; Álvaro Eseverri; Jose A. Aznar-Moreno; Stefan Burén; Luis M. Rubio
Sci Rep., 12(1): 10367
2022 | Journal article
DOI: 10.1038/s41598-022-14453-x
CONTRIBUTORS: Lucía Payá-Tormo; Diana Coroian; Silvia Martín-Muñoz; Artavazd Badalyan; Robert T. Green; Marcel Veldhuizen; Xi Jiang; Gema López-Torrejón; Janneke Balk; Lance C. Seefeldt; Stefan Burén; Luis M. Rubio