Old but memorable news from our previous website.

Jacqueline Séguin defends her MSc thesis!

20/08/15. Another student moves on to bigger and better things. Jacqueline successfully defended her MSc thesis entitled “Mechanistic Analysis of the Organophosphonate-Degrading Enzymes PhnY and PhnZ”. Well done Jacqueline!

DLZ attends ACS meeting in Boston

17/08/15. DLZ flew down to Boston to give a seminar in the ACS symposium held in celebration of Frank Raushel receiving the Gordon Hammes award. This award is given to researchers who have made outstanding contributions at the interface of chemistry and biology. Frank is a world leader in enzyme mechanisms and his lab recently conquered carbon-phosphorus lyase. Congratulations on this well earned award Frank!

Alyssa Brewer defends her MSc thesis!

14/08/15. Alyssa successfully defended her MSc thesis entitled “An Analysis of the Gene Cluster Encoding the Biosynthesis of the Fluorinated Natural Product Nucleocidin by Streptomyces calvus”. Great job Alyssa!

DLZ attends the 2015 ASP meeting at Copper Mountain, Colorado

29/07/15. DLZ headed into the Rocky Mountains to attend the 2015 American Society of Pharmacognosy (ASP) meeting where he gave a seminar entitled “A cure for baldness and cryptic biosynthesis in Streptomyces calvus“. Apart from raging headaches arising from the altitude of the resort (9000 ft!) and a few too many beer, DLZ had a great time and is very grateful to session organizer Katherine Ryan (UBC) for the invitation.

Alyssa Brewer wins ‘best seminar’ award at the 2015 CSC!

19/06/15. Alyssa won an award for best student seminar for her talk entitled “Raising the dead: Investigating the effect of the bldA gene on cryptic secondary metabolite production in Streptomyces calvus“. Alyssa was presenting in the excellent and well attended “Natural Product Biosynthesis” session of the 2015 CSC. Well done Alyssa! Fun fact: this is the third time a student from our lab has won a presentation award at the CSC!

Zechel lab attends the 2015 CSC in Ottawa

16/06/15. DLZ along with Jacqueline Séguin (MSc), Alyssa Brewer (MSc), David Simon (MSc) drove up to Ottawa for the annual Canadian Society for Chemistry meeting. Jacqueline gave a seminar on PhnY and PhnZ, Alyssa talked about the mysterious effects of the bldA gene on secondary metabolism in S. calvus, and David presented a poster on the effects of the bldA gene on the proteome of S. calvus. Great work guys!

Jacqueline Séguin receives an NSERC postgraduate award! 

30/08/14. Jacqueline (MSc) received a highly competitive NSERC award to support her graduate studies. Jacqueline is blazing a new trail with her work on the phosphonate catabolic enzymes PhnY and PhnZ. Well done Jacqueline!

Jacqueline Séguin and DLZ attend the 22nd ICPOC in Ottawa

11/08/14. The International Conference on Physical Organic Chemistry brings together scientists from around the world to discuss chemical mechanisms in a variety of contexts. DLZ had the privilege co-chairing the Enzyme Mechanisms session along with his old colleague Derek Pratt (U. of Ottawa).  Jacqueline (MSc) gave an excellent talk on her recent work on PhnY and PhnZ, a pair of enzymes that work together to degrade phosphonates.

XiMing Zhu defends his MSc thesis

06/08/14. Ming successfully defended his MSc thesis entitled “Exploration of cryptic biosynthetic pathways activated with a functional bldA gene in Streptomyces calvus”. Ming was a pioneer with his work on this old and unusual strain. Congratulations Ming!

DLZ visits Dublin for ICPC 2014

01/07/14. DLZ attended the 20th International Conference on Phosphorus Chemistry (ICPC) as an invited speaker. He presented our recent work on the new PhnY / PhnZ pathway for microbial degradation of organophosphonates, then found additional time to explore the many pubs of Dublin.

XiMing Zhu wins presentation award at the 2014 CSC

15/06/14. Ming won an award for his seminar on cryptic biosynthesis in S. calvus at the 2014 CSC in Vancouver! Congratulations Ming!

XiMing Zhu and DLZ attend the 2014 CSC in Vancouver

01/06/14. Ming (MSc) gave a great talk in the ‘Biosynthesis of Natural Products’ session of the 2014 Canadian Society for Chemistry annual meeting in his home town of Vancouver. The session was conveniently co-chaired by his boss, DLZ. Ming’s presentation covered our recent research on cryptic biosynthetic pathways in Streptomyces calvus. Later, DLZ flew the organophosphonate banner by giving a talk in the ‘Enzymology’ session on PhnZ, a new enzyme that cleaves carbon-phosphorus bonds.

Shane Colborne joins the lab

01/05/14.  Shane joins the group as a summer student to learn more about biosynthesis and enzyme catalysis. Welcome to the lab Shane!

Burning through carbon-phosphorus bonds

21/03/14.  Studies reported by the Zechel and Jia labs in the Proceedings of the National Academy of Sciences, USA havehave revealed  the molecular details of a new enzyme reaction that degrades organophosphonates. This follows hot on the heels of a complimentary study by researchers at Pennsylvania State University that was also published in PNAS. The enzyme, PhnZ, is found widely in marine bacteria and allows these organisms to extract inorganic phosphate (a life limiting nutrient) from organophosphonates. The Zechel lab previously reported that PhnZ is an iron dependent oxygenase. X-ray crystal structures of PhnZ obtained by Dr. Laura van Staalduinen from the Jia lab show that PhnZ uses two iron atoms to catalyze cleavage of a carbon-phosphorus bond. Along with the structural data, biochemical studies by Dr. Fern McSorley and Jacqueline Séguin from the Zechel lab indicate that one iron atom acts like a molecular vice to hold the substrate, while the second iron atom reacts with oxygen which then essentially burns through the carbon-phosphorus bond, releasing inorganic phosphate. These studies would not have been possible without substrate analogues that were chemically synthesized by Prof. Peter Wyatt (Queen Mary University of London) and Katharina Schiessl from the lab of Prof. Friedrich Hammerschmidt (University of Vienna).

Antibiotic production restored in a Streptomycete by curing baldness

24/10/13.  Research by M.Sc. student XiMing Zhu, former 4th year student Anjuli Szawiola, and visiting Ph.D. student Arne Gessner (from the Bechthold lab) figure prominently in the latest issue of Chemistry and Biology. The Streptomycesgenus of bacteria are renown as pharmaceutical factories, having afforded mankind the majority of drugs that are used today. Understanding the factors that trigger Streptomyces to product these compounds is necessary in order to discover new bioactive molecules. Most Streptomyces follow a fungus-like lifestyle and pass through a sporulation stage that affords a fuzzy appearance to bacterial colonies. The sproulation stage is also intimately tied to the production of bioactive molecules in the bacterium. Oddly, some Streptomyces do not sporulate and have a ‘bald’ appearance. Streptomyces calvus, discovered in the 1950’s is one of the oldest examples of a ‘bald’ streptomycete.  Research by the Zechel lab in collaboration with the labs of Andreas Bechthold (Albert-Ludwigs-Universität-Freiburg) and Gerry Wright (McMaster University) have discovered that the bald phenotype Streptomyces calvus is due to a point mutation in the bldA gene.  This gene is also essential for sporulation. Upon providing S. calvus with a correct copy of the bldA gene, sporulation was restored, and additionally a new antibiotic compound, called annimycin, was produced. A pioneer in the field ofStreptomyces genetics, Keith Chater, from the John Innes Centre (UK), provides a thought provoking commentary on our paper in the same issue of Chemistry and Biology.

Jacqueline Séguin receives a graduate studies scholarship!

15/10/13. Our new MSc student Jacqueline Séquin was the happy recipient of a Queen Elizabeth II Graduate Scholarship in Science and Technology. Well done Jacqueline!

Fern McSorley defends her doctoral thesis!

6/09/13. Fern McSorley successfully defended her Ph.D. thesis entitled “Enzymatic Cleavage of Carbon-Phosphorus Bonds“. During her time with the Zechel lab Fern played a key role in a number of pioneering studies involving the carbon-phosphorus lyase pathway (CP-lyase). CP-lyase has long attracted attention from chemists and microbiologists due to its global distribution in bacteria, its role in the global phosphorus cycle, and the novelty of the homolytic mechanism that is used to cleave the carbon-phosphorus bonds of its substrates. Fern also characterized a new oxidative CP-bond cleaving mechanism in a pair of marine enzymes, PhnY and PhnZ that are specific for the degradation of a common, naturally occurring, organophosphonate. This was a landmark finding as there were only two mechanisms known prior to her work. During her studies Fern had the opportunity to work with leading labs headed by Profs. Bjarne Hove-Jensen (University of Copenhagen), Zongchao Jia (Queen’s DBMS), Ed DeLong (MIT), Peter Wyatt (Queen Mary University of London), and Friedrich Hammerschmidt (University of Vienna). Fern’s research appears in 5 prominent journals, including JACS (2012and 2011), PNAS (2011), Biochemistry (2011), and PLoS-One (2012). Well done Dr. McSorley!

A whole bunch of new graduate students!

1/09/13. Big changes this month as the Zechel lab welcomes David Simon, Alyssa Brewer, and Jacqueline Sequin as new M.Sc. students. David will work jointly with the Oleschuk group to develop a microfluidic device to detect secondary metabolites in Streptomyces. Alyssa will investigate the biosynthesis of a peculiar polyketide called ‘annimycin’ that is produced by Streptomcyes calvus. Jacqueline will take on the mechanistic analysis of the newly discovered organophosphonate degrading enzymes PhnY and PhnZ, and will also engineer phosphotriesterases in collaboration with the Stan Brown group. Welcome all!

DLZ attends the CSC in Quebec City

29/05/13. DLZ attended the annual Canadian Society for Chemistry meeting where he presented 2 seminars on organophosphonate degrading enzymes and cryptic natural products in Streptomyces. He wishes the CSC would be held in Quebec every year!

Nathalie Butler joins the Zechel lab

1/05/13. Nathalie Butler, a Queen’s Biochemistry student, will join the Zechel lab as a summer student to work on a joint project with Prof. Stan Brown. Nathalie will investigate the substrate promiscuity of phosphotriesterases. Welcome Nathalie!

Usman Aftab joins the Zechel lab

10/04/13. The Zechel lab is pleased to welcome Usman Aftab as a visiting Ph.D. student. Usman hails from the lab of Prof. Imran Sajid in the Dept. of Microbiology and Molecular Genetics, University of the Punjab, Pakistan and is supported by a prestigious fellowship from the Higher Education Commission. During the next 7 months Usman will screen a variety of unique strains of Streptomyces that he collected in Pakistan for antitumor activity.

Aric Huang receives NSERC USRA!

20/02/13. Aric has received a prestigious NSERC research award which will support his studies in our lab this coming summer. Aric’s new summer project will involve the identification of new organophosphonate degradation pathways in pathogenic bacteria. Congratulations Aric!

Katie Groom successfully defends her doctoral thesis!

28/01/13. Katie led the way on a challenging project involving the Zechel and Snieckus labs that tackled the biosynthesis of indolocarbazoles and the chemical synthesis of indolocarbazole analogues. Indolocarbazoles are a diverse class of alkaloids derived from tryptophan that have attracted much interest in recent years for their anticancer properties. The biosynthesis of these molecules is equally interesting due to the novelty of some of the key reactions. Katie performed a groundbreaking study on one of the enzymes in this pathway, RebC, which performs a key oxidative reaction, in which she was able to identify the key active site amino acids involved in catalysis (ChemBioChem 2011). Her work was quickly followed by elegant studies by labs in Japan (Biosci. Biotechnol. Biochem. 2011) and the USA (Chem. Biol. 2012) that confirmed and expanded upon her findings. Well done Dr. Groom!

Zechel lab receives a new UPLC-MS

21/01/13. A new Waters Acquity UPLC-MS system has been installed in the Zechel lab. Purchased with the aid of anNSERC RTI1 grant, this instrument will allow the rapid separation of mixtures of molecules and their characterization by diode-array UV-visible spectroscopy and mass spectrometry. The UPLC-MS will support the natural product and enzymology studies in the Zechel lab, as well as research in the Petitjean, Jessop, Crudden, and Oleschuk labs. Students in these labs will have ready access to a state of the art instrument and receive extensive training and experience  with an analytical technique that is used widely in industry.

Welcome Aric Huang!

09/01/13. Aric is a 3rd year Chemical Biology student from McMaster University who will spend the next 4 months in our lab on a co-op term. Aric will work on characterizing new halogenases and modifying Streptomyces genomes with recombinases. Welcome Aric!

Welcome Arryana Carkner!

01/11/12. Arryana Carkner, a 1st year student at Queen’s, has joined the group to learn the ropes in a biological chemistry lab. Welcome to the team Arryana!

PhnO: Waste not, want not…..

3/10/12. The phnO gene of the phn operon encodes an enzyme that chemically modifies aminoalkylphosphonates. The role of this modification (specifically N-acetylation) in the context of the recently deciphered CP-lyase pathway was unknown – until now. Research led by Bjarne Hove-Jensen (PLoS One, 2012) has shown that for most aminoalkylphosphonates the phnO gene is dispensable and that these substrates can be processed by CP-lyase without modification. However, the simplest substrate, aminomethylphosphonate, cannot be processed by CP-lyase without modification by PhnO, suggesting that the proximity of a positively charged amino group to the CP bond of the substrate interferes with the CP bond cleaving activity of CP-lyase. A second surprise was that PhnO can detoxify a bacteriocidal substrate (S-1-aminoethylphosphonate, an analogue of D-alanine) which interferes with cell wall biosynthesis. The detoxified substrate is then processed by CP-lyase to provide inorganic phosphate for the cell. Waste not, want not indeed!

Welcome Anne Li!

09/09/12. Anne Li has joined the group to work on her 4th year thesis project. Anne will be using a genomic screening strategy to find new enzyme pathways that degrade organophosphonates. Welcome Anne!

Welcome XiMing Zhu!

01/09/12. Ming has joined the group to pursue a Master’s thesis in biological chemistry. Ming will endeavour to awaken ‘cryptic’ biosynthetic genes in Streptomyces calvus and characterize the encoded enzymes and natural products. Welcome to the team Ming!

Getting phosphate from phosphonate: Fern McSorley in the Spotlight!

20/06/12.  Fern McSorley’s elucidation of the new PhnY / PhnZ enzyme pathway for degradation of organophosphonates is featured in the latest issue of “Spotlights” in the Journal of the American Chemical Society. Well done Fern!

Welcome Arne Gessner!

02/06/12. Arne Gessner, a Ph.D. student from Andreas Bechthold’s lab, has joined our group for the next 2 months. Arne plans to dive deeply into biosynthetic pathways found in Streptomyces calvus, as well as look at ways to express cryptic pathways in other strains of Streptomyces.

DLZ and Fern McSorley attend the CSC

30/05/12. DLZ and Fern headed out west to Calgary for the Canadian Society for Chemistry annual meeting. Fern presented a talk on organophosphonate degradation by PhnY and PhnZ in the Metal Ions in Biology session, while DLZ attended an excellent Natural Products session where he presented research on activating cryptic biosynthetic pathways inStreptomyces.

Fern McSorley unlocks a secret for microbial life

10/05/12. All life forms need inorganic phosphate to survive. Day to day life as a microbe is especially hard because inorganic phosphate is scarce in soils and marine / aquatic environments. For this reason bacteria have evolved enzymatic pathways to obtain inorganic phosphate from other sources, including organophosphonates, which are characterized by a very stable carbon-phosphorus bond. Fern has characterized a new pair of enzymes, PhnY and PhnZ, that comprise a new pathway for carbon-phosphorus bond cleavage, joining the ranks of carbon-phosphorus lyase and ‘electron-sink’ enzymes like phosphonatase. PhnY and PhnZ both use ferrous iron to catalyze powerful oxidation reactions, thereby converting 2-aminoethylphosphonic acid to glycine (an amino acid) and inorganic phosphate. The PhnZ reaction is especially exciting as it represents a new enzyme mechanism. Fern’s work was just published in the Journal of the American Chemical Society. Well done Fern!

Welcome Stephanie Vanner!

2/05/12. Stephanie Vanner, a recent graduate of the highly regarded Chemical Biology program at McMaster University, has joined the Zechel  lab for the summer with a highly coveted NSERC summer research award. Stephanie will work on unlocking cryptic biosynthetic pathways in a species of soil bacteria called Streptomcyes.

Zechel lab awarded $150,000 for an LC-MS system

12/04/12. DLZ along with Profs. Cathleen Crudden, Philip Jessop, Richard Oleschuk, and Anne Petitjean were awarded $150 k by the Natural Sciences and Engineering Research Council of Canada (NSERC) to purchase an liquid chromatography mass spectrometer system. The LC-MS will play a crucial role in the search for new natural products by the Zechel lab.

DLZ visits the BioMOLAR Network

11/04/12. DLZ visited the BioMOLAR Network at the Dept. of Chemistry, University of Ottawa, where he spoke about carbon-phosphorus lyase and new enzymes that cleave CP bonds. Many thanks to Prof. Chris Boddy for organizing a great visit!

Anjuli Szawiola awarded 4th year thesis prize

9/04/12. Anjuli Szawiola won the Sullivan Prize for her 4th year thesis presentation entitled “Discovery of new bioactive molecules produced by Streptomyces calvus“. Well done Anjuli!

Welcome Christine Klaus!

12/03/12. Christine Klaus has joined the lab for a 4 month stay as an exchange student from the lab of Andreas Bechthold (Albert-Ludwigs-Universität-Freiburg). Christine hopes to crack the biosynthetic origins of natural products isolated fromStreptomyces calvus. Welcome to the group Christine!

CP-lyase in the news

15/02/12. Our work on CP-lyase, along with that of the Raushel lab, is the subject of a commentary in ChemBioChem.

Welcome Hanna Zhao!

9/01/12. Hanna is a 3rd year student in the highly regarded Chemical Biology program at McMaster University. She has signed on to a 4 month stint in our lab as a co-op student, during which time she will work on characterizing new halogenases.  Welcome to the group Hanna!

CP-lyase in the news.

24/11/11. Our recent PNAS 2011 paper describing the isolation of a soluble CP-lyase complex is featured on the Queen’s News Centre website.


At last, CP-lyase activity has been reconstituted in vitro!

17/11/11. Siddhesh Kamat, Howard Williams  Prof. Frank Raushel (Texas A&M University, College Station) finally knocked off one of the biggest challenges in mechanistic enzymology and recreated the CP-lyase reaction in a test tube. Published today in Nature, the work represents a tour de force in the reassembly a complex reaction pathway from individual enzymes that are, at best, borderline stable, when removed from the natural environment of the cell. Thanks to this work we now know that PhnI is a new type of nucleotide phosphorylase, catalyzing the formation of a-D-ribosyl-1-phosphonate-5-triphosphate from ATP and phosphonate. Consistent with the PhnGHIJK complex we described in ourPNAS 2011 paper, PhnI was only active in the presence of PhnGHL. Subsequently PhnM catalyzes the hydrolysis of the triphosphate, yielding a-D-ribosyl-1-phosphonate-5-phosphate. Finally, the long sought CP bond cleaving step was assigned to PhnJ, which was shown to be a  [4Fe-4S] dependent radical SAM enzyme. Reaction of PhnJ with a-D-ribosyl-1-phosphonate-5-phosphate cleaves the CP bond and yields the cyclic phosphate intermediate identified previously in ourJACS 2011 paper. The cyclic phosphate is proposed to derive from a covalent intermediate on PhnJ involving attack of the ribose 2-OH on a phosphothioester linkage to the enzyme. This is an attractive hypothesis, as it assigns a fundamental role to the 2-OH of ribose (anchimeric assistance) in the catabolism of phosphonates, as well as PhnP, the phosphodiesterase that hydrolyzes the cyclic phosphate. A door to an exiting new enzyme reaction has finally been opened, and for that we raise a glass to the Raushel lab and their magnificent achievement!

DLZ visits Dalhousie

29/09/11. DLZ headed out east to sample the great hospitality of the Dept. of Biochemistry and Molecular Biology at Dalhousie University. He gave a seminar on the discovery of ‘cryptic’ biosynthetic genes  in Streptomyces calvus and the discovery of a new natural product. DLZ thanks Prof. Stephen Bearne for arranging a very memorable visit, and the grad students of Biochemistry for a super lunch.

DLZ visits McMaster

22/09/11. DLZ had the privilege of visiting the Dept. of Chemistry at McMaster University to deliver a seminar on our recent findings in CP-bond cleaving enzymes. Special thanks goes to Prof. Philip Britz-McKibbin (a former schoolmate in DLZ’s undergrad and grad studies!) and his grad students for organizing an exceptional stay.

Welcome Anjuli and Matthew!

13/09/11. Anjuli Szawiola and Matthew Rankin-Byrne have joined the lab to work on their 4th year thesis projects. Anuli intends to characterize natural product biosynthetic pathways in Streptomyces calvus. Matthew will drive forward our research on new enzyme pathways involved in organophosphonate degradation.

New insights into the carbon-phosphorus lyase enzyme PhnP

16/08/11.  Last, but not least. Although PhnP is encoded by the final gene in the phn operon (phnCDEFGHIJKLMNOP), this enzyme does not play peripheral role in organophosphonate catabolism. A detailed analysis of the mechanism of this enzyme was performed using physical organic techniques, site-directed mutagenesis, and X-ray crystallography. The research findings by Shu-Mei He (M.Sc. 2008), Fern McSorley (Ph.D. student), Matthew Wathier and Matthew Wong (both former NSERC summer students), Kateryna Podzelinska (Ph.D. 2010, Jia lab), and Dr. Alemayehu Asfaw (postdoc, Beauchemin lab) have just been published in Biochemistry.

DLZ’s sabbatical report

08/08/11. description of DLZ’s adventures in Freiburg is now available. This was originally submitted as a report to the Ontario-Baden Württemberg Faculty Exchange program, which sponsored DLZ’s stay in Germany.


Fern McSorley awarded best presentation at CSC!

08/07/11.  Fern was awarded ‘best presentation’ by the Biological and Medicinal Chemistry Section of the Canadian Society for Chemistry annual meeting held in Montreal. She delivered a barn-burning seminar entitled “Mechanistic investigation of the biodegradation of an organophosphonate by PhnY and PhnZ”. Well done Fern!

DLZ returns to Queen’s

04/07/11.  DLZ has returned to Queen’s Chemistry after a fantastic sabbatical year with Andreas Bechthold at the Albert-Ludwigs-Universität in Freiburg, Germany. A special thanks goes to Andreas and his students for providing DLZ with a crash course in Streptomyces genetics, which spurred the discovery of the Zechel lab’s first natural product, ‘annimycin’!

CP-lyase: more secrets revealed.

20/06/11.  After nearly half a century of frustrated scientific investigation, an assembly of enzymes and proteins has been purified which may finally lead to the structure and mechanism of carbon-phosphorus lyase. This enzyme activity has long been pursued due to its unusual ability to cleave highly stable CP bonds (found in pharmaceuticals, herbicides, and chemical warfare nerve agents) at room temperature and neutral pH. Led by our super visiting professor Bjarne Hove-Jensen (University of Copenhagen) and Bjarne Jochimsen (Aarhus University), along with hard work by Fern McSorley from the Zechel lab, a soluble complex consisting of five proteins encoded by phnGHIJK was isolated through multiple purification steps. The results will appear in the early edition of Proceedings of the National Academy of Sciences, USA. Reconstruction of the CP-lyase reaction in vitro and X-ray crystallographic studies are now underway!

Fern McSorley and Katie Groom attend CSC

9/06/11. Ph.D. students Fern and Katie recently delivered well received seminars at the Canadian Society for Chemistry meeting held this year in Montreal. Fern presented hot off the press work on a new pair of organophosphonate degrading enzymes discovered through screening of marine metagenomic DNA, while Katie described her new findings on a key enzyme involved in the biosynthesis of a class of anticancer compounds called indolocarbazoles.

DLZ visits HIPS

30/05/11. DLZ had the privilege of visiting the Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS) in Saarbrücken, Germany, to deliver a seminar on flavin dependent enzymes in natural product biosynthesis. HIPS is dedicated to drug discovery from microbial natural products, drug optimization, and drug delivery. DLZ thanks Dr. Andriy Luzhetskyy and HIPS director Professor Rolf Müller for the tour of their stunning research facility and their warm hospitality fuelled by pizza and beer.


DLZ receives OBW award

21/04/11. DLZ is the grateful recipient of a Faculty Research Exchange award from the Ontario-Baden Württemberg Exchange Program. The award will help support DLZ’s sabbatical at the Albert-Ludwigs-Universtität Freiburg where he is studying natural product biosynthesis with Andreas Bechthold. The OBW program also provides support for Ontario university students to study in Germany. Check out the following link for more information: http://www.yorku.ca/ontbw/

Professor Hove-Jensen returns!

8/04/11. Welcome back Bjarne! Bjarne Hove-Jensen, who hails from the Dept. of Biology at the University of Copenhagen, has returned to our lab for more adventures in the world of organophosphonate degradation. During the next 6 months he hopes to elicit more secrets from carbon-phosphorus lyase.

DLZ visits University of Zürich

30/03/11. DLZ was delighted to return to his former haunt at the Biochemisches Institut, Universität Zürich, to deliver a seminar on our research on organophosphonate degradation by microbial enzymes. A special thanks goes to his former postdoc supervisor Prof. Andreas Plückthun for the invitation and the wonderful hospitality.


Carbon-phosphorus lyase

13/01/11. A major piece of a 50 year old puzzle has been found. The ubiquitous bacterial CP-lyase is a major contributor to the global phosphorus cycle through its ability to degrade organophosphonates. An effort spearheaded by our esteemed guest Prof. Bjarne Hove-Jensen and Fern McSorley (Ph.D. candidate) has delineated part of the pathway for organophosphonate degradation by CP-lyase (J. Am. Chem. Soc. 2011), as well as shed light on a possible mechanism for CP-bond cleavage.

Indolocarbazole biosynthesis

22/11/10. Research by Ph.D. candidate Katie Groom and postdoc Dr. Anupam Bhattacharya on one of the key enzymes involved in the biosynthesis of rebeccamycin and staurosporine has been accepted for publication in ChemBioChem. 

David Zechel is on sabbatical leave until July, 2011.

The boss will be away in Germany for the year, hidden away in the lab of Andreas Bechthold at the Albert-Ludwigs-Universität, Freiburg, Germany.

Ryan Latimer successfully defends M.Sc. thesis.

20/07/10. Ryan ably presented his work on the halogenase involved in the biosynthesis of chloramphenicol, which was published earlier this year in J. Mol. Biol.. Good job Ryan!

New funding for halogenase research.

01/07/10. Green Centre Canada (Queen’s University) has provided funding for developing halogenases as ‘green’ biocatalysts for the synthesis of organohalogens with drug-like properties.

An honoured guest!

15/02/10. We are very fortunate to have Professor Bjarne-Hove Jensen, from the Dept. of Biology, University of Copenhagen, to join group for a sabbatical stay until September. Bjarne hopes to crack the mechanism of carbon-phosphorus lyase during his time with us.

Chloramphenicol biosynthesis.

18/01/10. The X-ray crystal structure of CmlS, the halogenase that generates the dichloroacetyl moiety of the antibiotic chloramphenicol, is now in press (J. Mol. Biol. 2010, 397, 316-31). Chloramphenicol is a natural product produced by Streptomyces venezuelae that, upon its discovery in 1949, joined penicillin as one of the original ‘wonder drugs’ for fighting long-time scourges of mankind, including typhus. This was a great effort by Kateryna Podzelinska (Jia lab, Queen’s Biochemistry) who solved the structure, and Ryan Latimer (Zechel lab) who discovered a covalently bound flavin cofactor.

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