Ruthenium Organometallic Complexes
Lead Research Organisation:
UNIVERSITY OF CAMBRIDGE
Department Name: Chemistry
Abstract
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Organisations
People |
ORCID iD |
| Paul Barker (Primary Supervisor) | |
| George Biggs (Student) |
Publications
Biggs G
(2020)
Unlocking the Full Evolutionary Potential of Artificial Metalloenzymes Through Direct Metal-Protein Coordination A review of recent advances for catalyst development
in Johnson Matthey Technology Review
Biggs GS
(2021)
Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naïve Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation.
in Angewandte Chemie (International ed. in English)
Biggs GS
(2019)
Use of a fluorinated probe to quantitatively monitor amino acid binding preferences of ruthenium(ii) arene complexes.
in Dalton transactions (Cambridge, England : 2003)
Studentship Projects
| Project Reference | Relationship | Related To | Start | End | Student Name |
|---|---|---|---|---|---|
| EP/N509620/1 | 30/09/2016 | 29/09/2022 | |||
| 1800459 | Studentship | EP/N509620/1 | 30/09/2016 | 29/09/2020 | George Biggs |
| Description | This research has focussed around two biological applications of ruthenium organometallic complexes, their use as cytotoxic agents in the treatment of cancer and how they can be introduced into the active site of engineered enzymes to develop artificial metallo-enzymes. To address the first application, we have developed a spectroscopic approach, using NMR, to monitoring the speciation of ruthenium complexes in complex amino acid mixtures. This information will aid scientists in the design on new ruthenium anti-cancer drugs, which have currently failed to pass clinical trials, due to a lack of understanding of how and where they bind in a complex biological environment. To address the second application, we have explored the ligand exchange behaviour of different ruthenium complexes when they bind to different proteins. We have developed a method to control the metal coordination environment when binding to proteins. We have had particular success in coordinating ruthenium complexes to the four-helical bundle protein cytochrome b562 and gratifyingly we have observed catalytic activity in these ruthenium protein hybrids. Artificial metallo-enzymes, can have unique catalytic capabilities which can be very beneficial in synthetic biology. In particular we have seen success with these artificial metalloenzymes as catalyst for transfer hydrogenation which is a very relevant reaction in many industries including the pharmaceutical industry. This research has very much achieved the goals set out at the beginning of the award. |
| Exploitation Route | The findings from the project so far have led to the completion of a number of successful undergraduate research projects. Furthermore, this research has also formed the basis for a successful PhD application, which will explore the evolutionary potential of artificial metallo-enzymes generated by direct metal-protein coordination. |
| Sectors | Chemicals Healthcare Pharmaceuticals and Medical Biotechnology |