People
Dr Patricia Rodríguez Maciá
Lecturer in Chemistry
School/Department: Chemistry, School of
Email: prm28@leicester.ac.uk
Profile
Patricia studied Chemistry at the University of Alicante in Spain, before moving to Germany for her PhD at the Max Planck Institute for Chemical Energy Conversion (MPI-CEC, Muelheim) with Prof. Wolfgang Lubitz, where she worked with hydrogenases and bio-inspired catalysts for hydrogen conversion. She then conducted her first postdoctoral research at MPI-CEC with Prof. Serena DeBeer. In 2020, she joined the University of Oxford as a PDRA in Prof. Kylie Vincent’s group. Patricia started her independent career in 2021, when she was appointed Glasstone Research Fellow in the Department of Chemistry at the University of Oxford. In 2023, she moved to the University of Leicester to take up a Lecturer (Assist, Prof,) position in the School of Chemistry and the Leicester Institute for Structural and Chemical Biology, where she leads a small group doing research on natural and artificial metalloenzymes for small molecule activation. Patricia is the EDI Lead for Chemistry. Patricia’s work has been recognised by prestigious prizes such as the Ernst-Haage prize for outstanding achievements in the field of chemical science and the RSC IBDG 2022 Early Career Researcher Award, naming her as a rising star in bioinorganic chemistry.
Research
The research in the PRM lab focuses on biocatalysis, to learn from and mimic nature at the intersection of chemistry, biology, and materials science. The overall goal is to establish fundamental chemical insight for supporting future renewable energy technologies, i.e. to develop efficient (biohybrid) catalysts and new catalytic routes for energy conversion reactions based on abundant and cheap metals. Energy-converting metalloenzymes are capable of using earth-abundant metals in their active site to perform key chemical transformations, such as the activation of small molecules, e.g. N2, H2, CO, O2, in a very efficient manner. These reactions still represent big challenges for industry, and it is often difficult to produce synthetic catalysts with efficiencies and selectivity similar to the natural metalloenzymes.
The PRM lab combines the fields of biology, synthetic chemistry and physical chemistry to study energy-converting metalloenzymes and understand the chemistry at their active site. Solutions to the energy problem require a fundamental understanding of how energy conversion processes happen in nature and of what it takes to make catalytic systems with performances and efficiencies as high as the systems existing in nature (i.e. energy converting metalloenzymes), while maintaining the relative simplicity of a molecular catalyst or catalytic material. Thus, the research in the PRM lab is dedicated to translating the understanding of complex biocatalytic processes into catalyst design for technological applications.
Metalloenzymes for energy conversion: study and exploitation of biocatalytic systems
We are passionate about investigating the catalytic mechanism of natural metalloenzymes which activate small molecules such as H2, CO2, N2 and O2 in nature. We mainly work with hydrogenases (H2 oxidation and production) and CO dehydrogenases (reversible CO2-to-CO conversion). We use a combination of spectroscopic, electrochemical, computational and structural methods to understand at the molecular level the chemistry at the active site as well as the interplay between the active site and protein matrix. The overarching aim is to develop design principles to build new biohybrid systems for applications in green chemistry.
Design and characterisation of Artificial Metalloenzymes (ArMs) for small-molecule activation based on natural and artificial protein scaffolds
We use the knowledge gained from the natural systems to employ a ‘mechanistically-driven’ approach to design novel artificial metalloenzymes (ArMs) for green chemistry (H2 production, CO2 reduction, O2 activation, water splitting, N2 reduction and oxidation reactions). ArMs are biohybrid catalysts in which a synthetic catalysts is embedded inside a protein scaffold. The protein scaffold is used to fine tune the properties and the chemistry of the active site. This approach can be also used for rapid screening of mutant libraries to generate systems with desirable features such as oxygen tolerance, enhanced catalytic performance, or enhanced temperature sensitivity. We use natural proteins as well as de novo designed proteins as scaffolds for our ArMs. The ArM systems are screen for activity and mechanistically investigated using electrochemistry alongside spectroscopic and structural techniques. We are also interested in exploring new-to-nature reactions with our ArMs
For more information visit the PRM group website: https://www.rodriguezmacialab.com/.
Collaborative institutions and universities
Diamond Light Source (UK), Centre Laser Facility (UK), Max Planck Institute for Chemical Energy Conversion (Germany), Pacific Northwest National Laboratory (USA), SPring-8 (Japan), Bochum University (Germany), Uppsala University (Sweden), University of Birmingham (UK), University of Nottingham (UK), University of Oxford (UK), University of Essex (UK).
Publications
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The missing pieces in the catalytic cycle of [FeFe] hydrogenases, Manon T. Lachmann, Zehui Duan, Patricia Rodríguez-Maciá, James A. Birrell, Chemical Science 2024,15, 14062-14080.
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Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases, Martini, M.A., Bikbaev, K., Pang, Y., Lorent, C., Wiemann, C., Breuer, N., Zebger, I., DeBeer, S., Span, I., Bjornsson, R., James A. Birrell and Patricia Rodríguez-Maciá *, Chemical Science 2023, 14, 2826-2838.
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Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase ‘Hyd-2’ from Escherichia coli, Rhiannon M. Evans, Stephen E. Beaton, Patricia Rodriguez Macia, Yunjie Pang, Kin Long Wong, Leonie Kertess, William K. Myers, Ragnar Bjornsson, Philip A. Ash, Kylie A. Vincent, Stephen B. Carr, and Fraser A. Armstrong, Chemical Science 2023, 14, 8531-8551.
- Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima, N.Chongdar, P. Rodríguez-Maciá, E.J. Reijerse, W. Lubitz, H. Ogata, J.A. Birrell, Chemical Science 2023, 14, 3682-3692.
- Bioelectrocatalytic CO2 reduction by redox polymer-wired carbon monoxide dehydrogenase gas diffusion electrodes, J.M. Becker, A. Lielpetere, J. Szczesny, J.R.C. Junqueira, P. Rodríguez-Maciá, J.A. Birrell, F. Conzuelo, W. Schuhmann, ACS applied materials & interfaces 2022, 14, 46421-46426.
- Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site, M. Lorenzi, J. Gellett, A. Zamader, M. Senger, Z. Duan, P. Rodríguez-Maciá, G. Berggren, Chemical Science 2022, 37, 11058-11064.
- The catalytic cycle of [FeFe] hydrogenase: A tale of two sites, J.A. Birrell, P. Rodríguez-Maciá, E.J. Reijerse, M.A. Martini, W. Lubitz, Coordination Chemistry Reviews 2021, 449, 214191.
- The Nonphysiological Reductant Sodium Dithionite and [FeFe] Hydrogenase: Influence on the Enzyme Mechanism, M.A. Martini, O. Rüdiger, N. Breuer, B. Nöring, S. DeBeer, P. Rodríguez-Maciá, J.A. Birrell, Journal of the American Chemical Society 2021, 143, 18159-18171.
- A Beginner's Guide to Thermodynamic Modelling of [FeFe] Hydrogenase, J.A. Birrell, P. Rodríguez-Maciá, A. Hery-Barranco, Catalysts 2021, 11, 238.
Teaching
Patricia teaches Chemistry BSc and MChem degrees Modules: Introduction to Inorganic Chemistry CH1202 (Module Lead) and Advance Structural Characterisation CH4201. She also teaches Inorganic Chemistry tutorials for Y1 and Y2 Leicester and DLI students.
Awards
2022: RSC IBDG Early Career Award (Royal Society of Chemistry & Inorganic Biochemistry Discussion Group) for interdisciplinary approaches to study mechanism of metalloenzymes with particular focus on [FeFe] hydrogenases. Named ‘future star in the field of bioinorganic chemistry’
2021: Glasstone Research Fellow in Science (University of Oxford)
2020: E P A Cephalosporin Junior Research Fellowship (Linacre College & University of Oxford)
2017: Ernst Haage Prize for Doctoral Students. Best Dissertation 2017. (Max Planck Society & Ernst Haage Foundation)
2016: Best Poster Award. XXI International Hydrogenase Conference, Marseille (France)
2015: Best Poster Award. XXIII International Symposium on Bioelectrochemistry and Bioenergetics, Malmö (Sweden)
2014: Max Planck Scholarship for PhD students
2013: Max Planck Scholarship for internship
2012: Leonardo Da Vinci Scholarship
2010/11: Erasmus Scholarship