Bumper Viva Success
Congratulations to all the PhD students who successfully passed their vivas this year. Well done to Toby Hedisaon, Kang Cheng, Claudio do Santos, and Alex Geddes.
"Better than Nature"
Our latest paper on H-tunneling with 'Better than Nature' biomimetic coenzymes out in JACS today: Donor–Acceptor Distance Sampling Enhances the Performance of “Better than Nature” Nicotinamide Coenzyme Biomimetics
Congratulations to MAGIC PhD students Sylwia Czarnota and Andreea Iorgu who won prizes for the best teaser talk and best poster respectively at the 1st Biophysical and Biochemical one-day Symposium hosted by the ResoN8 FM group .
Alcohols to amines: the clean, green way!
We report how alcohol and amine dehydrogenases can work together to convert alcohols to amines. Ammonium is the only input and water the only by-product making this reaction compatible with the enzyme's natural aqueous environment - an excellent feature for a synthetic biology process. You can read about the work, published in the journal Science, here: Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades
Synthetic Biology: Hope or Hype?
PhD student Uzma Choudry has had a popular science article explaining synthetic biology published on the Naked Scientists website. If you're new to the field why not have a read here
Two new Nature papers about ubiquinones and related decarboxylase proteins.
We report that UbiX produces a novel flavin-derived cofactor which is required for both the decarboxylase activity of UbiD and the reversible decarboxylaser activity of Fdc1. You can read about the work here: New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition and here: UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis
MIB wins £10.3 million for Synthetic Biology Research Centre
Manchester Institute of Biotechnology (MIB) will receive £10.3 million to set up the Centre for Synthetic Biology of Fine and Speciality Chemicals (SYNBIOCHEM). The Centre will develop new products and methods for drug discovery and production, focussing on new antibiotics, and agricultural chemicals, including herbicides and insecticides, as well as new materials for sustainable manufacturing. Nigel Scrutton, Co-Director of SYNBIOCHEM, says the grant is a significant win for Manchester: “Our vision is to harness the power of Synthetic Biology (SynBio) to propel chemicals and natural products production towards ’green’ and sustainable manufacturing processes. More broadly, the Centre will provide the general tools, technology platforms and SynBio 'know-how' to drive academic discovery and translate new knowledge and processes towards industrial exploitation. It will see our world class researchers using bacteria to produce chemicals to make everyday products like toothbrushes and credit cards, which are currently made from unsustainable fossil fuels. Not only will this help improve people’s everyday lives in the future but it will support long-term economic growth.”For more details see the SYNBIOCHEM website.
MIB wins £3 million grant for cutting edge biotechnology harnessing the power of SynBio
Professor Nigel Scrutton and his team at the Manchester Institute of Biotechnology are one of five beneficiaries of the BBSRC’s Strategic Longer and Larger Grants (sLoLaS) scheme which funds high-value long-term research projects. The combined effect of fossil carbon depletion and climate change are forcing humankind to replace fossil fuels with cleaner more sustainable forms of energy as we tackle the demands of an ever increasing and ageing population, affordable healthcare provision, resource efficiency, food security and energy shortages. Fossil fuels currently provide the raw material for the manufacture of many everyday products that we take for granted including pharmaceuticals, food and drink, plastics and personal care. This 5 year research programme is at the heart of this agenda developing bio-based SynBio technology to deliver bespoke SynBio solutions for chemicals/natural products synthesis that are smart, predictable and sustainable.
Magnetic fields are unlikely to effect the radical pair mechanism in redox enzymes.
Our work on magnetic field effects and human health, in which we we concluded that thermally driven, flavoenzyme-catalysed reactions are unlikely to be influenced by exposure to external magnetic fields, is in top 5% of all articles (98%ile) ever tracked by Altmetric as well as being reported in the Telegraph and discussed on NHS Choices. You can read the full open access article here
BBSRC Alert 14
We have just been awarded a BBSRC Alert 14 grant to establish a multi-purpose ultrafast spectroscopy instrument to support a wide range of programmes in the UK bioscience community. The instrument will have a wide range of capabilities including UV-visible and IR transient absorption, and fluorescence up-conversion. For more details see here.
Congratulations to Nicole Leferink and Toby Hedison who won poster prizes at the 18th International Symposium on Flavins and Flavoproteins for their posters titled "Nitric oxide synthase catalysis is associated with a 'rugged' energy landscape" and "Conformational kinetics of Homo sapiens cytochrome P450 reductase" respectively. For more photos from the symposium see here.
Distant residues remote from the active site can have marked effects on enzyme catalysis
With our collaborators in Liverpool we've shown that show that improving the accessibility of the active site pocket of copper nitrite reductase by mutation of a surface-exposed phenylalanine residue (Phe306), located 12Å away from the catalytic site type-2 Cu (T2Cu), profoundly affects intra-molecular electron transfer, substrate-binding and catalytic activity.
You can read about the work in Nature Communications: Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase
Our EMBO conference on "Enzyme mechanisms by biological systems" brought together leading European and US enzymologists working on biological catalysis, mechanisms and systems. We receive an excellent report from EMBO with many positive comments on the quality of our speakers and the diversity of the programme. The conference dinner at Tatton Park was rather good too!
Happy Birthday to Nigel!
2 vivas in 2 days and 2 new PhDs from the lab! Well done Anna and Marta.
Congratulations to PhD student Anna Hauck for winning the best poster prize for her poster titled "Analysis of a cyanobacterial tetrapyrrole photocycle" at the Tetrapyrrole Discussion Group Meeting held at the University of Kent.
Exciting breakthrough in search for neurodegenerative disease treatments
We have detailed how an enzyme in the brain interacts with an exciting drug-like lead compound for Huntington’s Disease to inhibit its activity. The findings demonstrate that it can be developed as an effective treatment for neurodegenerative diseases. The research is published in the journal Nature.
Structural basis of kynurenine 3-monooxygenase inhibition. Marta Amaral, Colin Levy, Derren J. Heyes, Pierre Lafite, Tiago F. Outeiro Flaviano Giorgini, David Leys & Nigel S. Scrutton, Nature, 496, 382–385, (18 April 2013)
“MAGIC” brings Marie Curie success to Manchester worth 3.4 million Euros
The MIB and PSI (PI: Nigel Scrutton) have secured a Marie Curie FP7 IDP training network grant worth 3.4 million euros. The four year grant entitled “MAGnetic Innovation in Catalaysis” will see the MIB and PSI host 12 Early Stage Researchers (ESR’s) who will be appointed to three-year PhD training programmes. This project will see Manchester partner with six Universities (Tokyo, Freiburg, Lund, Joseph Fourier in France, Edinburgh and Copenhagen) and five companies (AZ, Bruker, TGK, Conformetrix, and SarOMICS). Each ESR will be closely linked to the international and industrial partners who will be actively involved in their research projects. The concept of team-based activity is well founded across research groups in MIB-PSI and will enrich the training experience bringing multiple skills embedded in these teams to MAGIC programmes.
The aim of the MAGIC Innovative Doctoral Programme is to train the future generation of leading investigators of biological catalysis/enzymology with a view to developing new enabling technologies that can advance physical understanding of catalysis and mechanism. Collaborative research projects will explore the mechanistic details of enzyme systems by adopting innovative, versatile and unique experimental techniques to probe the contributions of motions across multiple spatial and temporal timescales and quantum chemical effects. These novel methods will transform current experimental capabilities and will be applied to a range of important biological catalysts to probe the mechanistic importance of coupled motions and quantum physico-chemical effects.
Updated structure of Drosophila cryptochrome
MIB investigators David Leys, Nigel Scrutton along with Colin Levy (SEO crystallography) and Alex Jones (PSI Fellow) have reported an important revision of the Drosophila cryptochrome structure which has major implications for the presumed biological function of the protein. The original structure was published in Nature by the Crane group in 2011, but the Manchester team identified major problems with the original reported structure. Subsequently, and working with the Crane group, the MIB team have now published a revised structure which appeared in the March 21 edition of Nature (Updated structure of Drosophila cryptochrome doi:10.1038/nature11995).