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2018 Speakers

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Emily Balskus

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Emily Balskus

Morris Kahn Associate Professor of Chemistry and Chemical Biology
Harvard University

 

Emily Balskus

Emily is originally from Cincinnati, Ohio, where she first became interested in chemistry as a high school student. She graduated from Williams College in 2002 as valedictorian with highest honors in chemistry. After spending a year at the University of Cambridge as a Churchill Scholar in the lab of Prof. Steven Ley, she pursued graduate studies in the Department of Chemistry and Chemical Biology (CCB) at Harvard University, receiving her PhD in 2008. Her graduate work with Prof. Eric Jacobsen focused on the development of asymmetric catalytic transformations and their application in the total synthesis of complex molecules. From 2008–2011 she was an NIH postdoctoral fellow at Harvard Medical School in the lab of Prof. Christopher T. Walsh. Her research in the Walsh lab involved elucidating and characterizing biosynthetic pathways for the production of small molecule sunscreens by photosynthetic bacteria. She also received training in microbial ecology and environmental microbiology as a member of the Microbial Diversity Summer Course at the Marine Biology Lab at Woods Hole during the summer of 2009.

Emily joined the CCB faculty in 2011 and is currently the Morris Kahn Associate Professor of Chemistry and Chemical Biology. She is also an Associate Member of the Broad Institute of Harvard and MIT, a Faculty Associate of the Microbial Sciences Initiative at Harvard, a member of the Harvard Digestive Diseases Center, and a member of the MIT Center for Microbiome Informatics and Therapeutics. Her independent research has been recognized with multiple awards, including the 2011 Smith Family Award for Excellence in Biomedical Research, the 2012 NIH Director’s New Innovator Award, and the 2013 Packard Fellowship for Science and Engineering. She was selected as one of MIT Technology Review’s 35 Innovators Under 35 in 2014 and in 2016 was named an HHMI-Gates Faculty Scholar.

Learn more about Dr. Balskus and the Balskus Lab here.

Vahe Bandarian

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Vahe Bandarian

Professor
University of Utah

 Vahe Bandarian

Vahe Bandarian (b. 1970) received his BS degree in Biochemistry from the California State University in Los Angeles in 1992.  He received his PhD in Biochemistry in 1998 from the University of Wisconsin-Madison working under the direction of George Reed.  After carrying out postdoctoral studies with Rowena Matthews at the University of Michigan in Ann Arbor he joined the faculty of the Department of Biochemistry at the University of Arizona in 2003.  In 2015 he moved as Professor of Chemistry to the University of Utah.  Vahe’s lab studies biosynthetic pathways to natural products that include modified nucleic acids and peptides.  His contributions have been recognized by a Burroughs Wellcome Career Award in Biomedical Sciences and the Pfizer Award in Enzyme Chemistry by the Division of Biological Chemistry at ACS. 

 

Learn more about Dr. Bandarian here.
 
Learn more about the Bandarian Research Group here.

Theodore Betley

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Theodore Betley

Professor of Chemistry and Chemical Biology
Harvard University

 
Theodore Bentley

Ted was born in 1977.  He earned his B.S.E. in Chemical Engineering from the University of Michigan in 1999.  He received his PhD in Chemistry from Caltech under Jonas Peters in 2005.  After a postdoctoral stint with Dan Nocera at MIT, he started his independent career at Harvard in 2007 when he is currently a Professor of Chemistry and Chemical Biology.

 

Learn more about the Betley Lab here.

Thomas Brunold

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Thomas Brunold

Professor
University of Wisconsin - Madison

 Thomas Brunold

Thomas C. Brunold was born in Bern, Switzerland, in 1969. He received his Ph.D. from the University of Bern in 1996, working with Hans U. Güdel on the design and spectroscopic characterization of new transition-metal based near-IR laser materials.  From 1997 to 1999, he was a postdoctoral fellow with Edward I. Solomon at Stanford University, studying binuclear iron and manganese centers in proteins and synthetic model complexes.  He joined the faculty at the University of Wisconsin-Madison in 1999. His research interests include spectroscopic and computational studies of metalloenzymes (e.g., thiol dioxygenases) and metal-containing cofactors (such as coenzyme B12).

 

Learn more about Dr. Brunold here.

Learn more about The Brunold Research Group here.

Nick Cox

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Nick Cox

Senior Lecturer
Research School of Chemistry,
Australian National University

Nicholas Cox

 

Nick Cox completed his Ph.D. at the Australian National University (ANU) in 2008.  He then moved to Max Planck Institute for Bioinorganic Chemistry as a Postdoc (2009 - 2010) and later as a group leader (2011 - 2015) after the institute was re-established as the Max Planck Institute for Chemical Energy Conservation.  He returned to the Research School of Chemistry at ANU at the start of 2016 as a Future Fellow.  His research is focused on the study of enzymes using both magneto-optical and magnetic resonance techniques.

 

Learn more about Dr. Cox's research group here.

Marcetta Darensbourg

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Marcetta Darensbourg

Professor of Chemistry
Texas A&M University

 Marcetta Darensbourg

Marcetta York Darensbourg was born and raised by her schoolteacher parents in the small hamlet of Artemus, Kentucky, on the banks of the Cumberland River.  As did her parents, she graduated from Union College in the nearby Barbourville, Ky.  Encouraged by her professors there, she pursued graduate studies in Inorganic Chemistry at the University of Illinois, Champaign/Urbana, receiving a Ph.D. in 1967 under the mentorship of Professor Theodore L. Brown.  While in graduate school she met Donald Darensbourg, also an Inorganic Chemist.  Her first appointments were short term lectureships at Vassar College, followed by SUNY Buffalo; in 1971 she was appointed assistant professor at Tulane University where she and Don rose through the ranks, moving to Texas A&M as Full Professors in 1982.  She holds the title of Distinguished Professor of Chemistry.  She lectures undergraduate and graduate courses devoted to inorganic and organometallic chemistry.

 

Marcetta’s research trajectory has mirrored developments in transition metal organometallic chemistry, specifically in the synthesis and characterization of carbon monoxide-stabilized, electron-rich metal hydrides and mechanisms of hydride transfer to organic substrates.   Intrigued by the possibility of metal hydrides in nature, specifically in the active sites of the hydrogenases, she directed efforts towards biomimetics of those sites and towards using the tools of organometallic chemistry to link the synthetic analogues with the natural hydrogen processing biocatalysts.  Other metalloenzyme active sites that perform carbon-carbon coupling processes add additional inspiration for research into nature’s design for eliciting catalysis by earth abundant metals in cases where the chemical industry relies on rare and expensive noble metals.  Her research has resulted in >250 peer reviewed publications as well as multiple awards including the American Chemical Society’s Award in Organometallic Chemistry (2017), and the ACS Award for Distinguished Service in the Advancement of Inorganic Chemistry (1996).  She is a member of the National Academy of Science (2017), and a fellow of the American Academy of Arts and Sciences, the Royal Society of Chemistry and the American Chemical Society.    She has mentored > 50 students to the Ph.D. degree in Chemistry.

Learn more about M.Y. Darensbourg Research Laboratories here.

Petra Fromme

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Petra Fromme

Director and Professor,
Biodesign Center for Applied Structural Discovery
Arizona State University

 Petra Fromme

Dr. Fromme received her masters at the Free University in Berlin in Biochemistry (1985) and then received her doctorate in Chemistry at the Technical University in Berlin (1988) where she then became a professor in 1992.  During this time she developed and pursued her fascination with understanding the function of membrane proteins by investigating and determining their atomic structures.  In 2002, Dr. Fromme joined Arizona State University as a professor of Chemistry and Biochemsitry where she has worked with distinguished colleagues from around the world to pioneer a new technique for imaging proteins using extraordinarily powerful x-ray lasers that has the capability to make movies of these fascinating proteins in action.

Birthplace:
Berlin, Germany

Research Area:
Dr. Fromme uses ultrafast x-ray laser pulses to take pictures of nature’s molecular machines called proteins to understand how they work. Many of these proteins are involved in disease and useful for solar energy conversion, so her discoveries will help us to design better drugs and clean energy systems for a brighter future.

Career Highlight:
Dr. Fromme determined the atomic structure of the largest protein to date called Photosystem I, which is responsible for capturing and storing solar energy in plants and algae.

Fun Fact:
Dr. Fromme plays the viola in the Tempe Symphony Orchestra and Scottsdale Philharmonic.

 

Learn more about The Fromme Group here.

Learn more about the Biodesign Center for Applied Structural Discovery here.

Learn more about Dr. Fromme here.

Michael T. Green

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Michael T. Green

Professor of Chemistry, School of Physical Sciences
Professor of Molecular Biology & Biochemistry, School of Biological Sciences
University of California, Irvine

Michael T. Green

Education:

  • B.S. Chemistry, B.S. Physics, Texas A&M University, 1992
  • M.S. Chemistry, The University of Chicago, 1994
  • Ph.D. Chemistry, The University of Chicago, 1998
  • Burroughs-Wellcome Postdoctoral Fellow, California Institute of Technology, 1998-2001
  • National Institutes of Health Postdoctoral Fellow, California Institute of Technology, 2000-2002


Honors and Awards:

  • Dillon Steele Lecturer, University of Queensland, Brisbane, Australia, 2015
  • American Association for the Advancement of Science Fellow, 2014
  • Honored for distinguished contributions to the field of bioinorganic chemistry, particularly in the elucidation of structure function relationships critical to biological C-H bond activation
  • Alfred P. Sloan Research Fellow, 2006
  • Beckman Young Investigator Award, 2004
  • National Science Foundation Career Award, 2004
 
Learn more about The Green Group here.

Robert Hausinger

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Robert Hausinger

Professor of Microbiology & Molecular Genetics and Biochemistry & Molecular Biology
Michigan State University
Robert Hausinger

Dr. Hausinger is a Professor of Microbiology and Molecular Genetics as well as Biochemistry and Molecular Biology at Michigan State University.  His laboratory investigates microbial physiology and enzymology related to transition metals.  Current areas of emphasis include:

  • Assembly and mechanism of the nickel-pincer cofactor of latate racemase
  • roles and mechanisms of several 2-oxoglutarate-dependent oxygenases
  • Activation of urease

 

Learn more about Dr. Hausinger here.

Donald Hilvert

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Donald Hilvert

Professor of Organic Chemistry
ETH Zurich

 Donald Hilvert

Donald Hilvert has been full Professor at the Organic Chemistry Laboratory of ETH Zurich since October 1, 1997. His group is developing general strategies for the design of proteins with customized catalytic properties. The aim is to gain a better understanding of the molecular origins of the catalytic powers of natural enzymes and their selectivity. Beyond that artificial biocatalysts may be useful in research, medicine and industry.

Professor Hilvert was born in 1956 in Cincinnati, Ohio, USA, and obtained his B.A. from Brown University, Rhode Island, in 1978. He earned his Ph.D. from Columbia University, New York, in 1983, with a dissertation under the supervision of Prof. R. Breslow. Following a postdoctoral work with Prof. E.T. Kaiser at Rockefeller University, New York, he joined the Scripps Research Institute as an assistant professor in 1986, where he was named associate professor in 1989 and full professor in 1993. He came to ETH Zurich as full Professor of Organic Chemistry in 1997. 

Donald Hilvert was awarded the Alfred P. Sloan Research Fellowship in 1991-93, the Arthur C. Cope Scholar Award of the ACS in 1992, and the Pfitzer Award in Enzyme Chemistry in 1994.

Learn more about the Hilvert/Kast Group here.

 

Roland Lill

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Roland Lill

Institut für Zytobiologie
Philipps-Universität Marburg

 
Roland Lill

Roland Lill received his diploma in Biochemistry in 1981 from the University of Munich.  Lill stayed at the University of Munich and took the position of Research Assistant from 1982-1985 and then his Post-doctoral Fellowship from 1986-1987.  Lill went on to continue his Post-doctoral Fellowship at the University of California, Los Angeles from 1987-1989.  He returned to the University of Munich and became a Senior Research Assistant from 1990-1996.  In 1996 he took the position of Associate Professor at Universität Marburg and would become a full professor in 2002.  Dr. Lill has remained at Universität Marburg since and has focused his research on Biosynthesis of cellular iron-sulfur proteins and Mechanisms of cellular iron regulation.

Research in his group concentrates on the molecular mechanisms of the biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes. These proteins contain Fe/S clusters as inorganic co-factors, and they participate in electron transfer reactions, enzyme catalysis and the regulation of various cellular processes. Important cellular processes such as respiration, citric acid cycle, numerous metabolic reactions, DNA synthesis and repair, ribosome biogenesis, tRNA modification and iron regulation require assistance of these ancient protein cofactors. Assembly of the Fe/S clusters and their insertion into apoproteins in a living cell is a complex process involving more than 25 proteins. The mitochondrial ISC assembly machinery (see Figure) was inherited from bacteria and is involved in biogenesis of all cellular Fe/S proteins, i.e. proteins in mitochondria, cytosol and nucleus. Maturation of extra-mitochondrial proteins additionally needs components of the mitochondrial ISC export machinery and proteins of the cytosolic CIA machinery. According to a model mitochondria export a factor (X in Figure) which is essential for Fe/S protein biogenesis in the cytosol by the CIA machinery.

Another topic of his research is the intracellular compartmentalization and regulation of iron. In particular, we are interested in the components and mechanisms involved in iron transport and regulation in mitochondria. Mitochondrial import depends on reduced (ferrous) iron, a membrane potential, and involves the mitochondrial carrier proteins Mrs3/Mrs4 (see Figure). Additional iron transporters remain to be identified. Defects in mitochondrial ISC components result in an increased cellular iron uptake and in iron accumulation in mitochondria. The molecular basis underlying the (dys)regulation of cellular iron compartmentation as a result of Fe/S protein defects is unclear to date.

 

Learn more about Dr. Lill here.

Connie Lu

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Connie Lu

Associate Professor of Chemistry
University of Minnesota, Twin Cities

 
Connie Lu

Connie Lu received her B.S. in Chemistry from MIT in 2000 and her Ph.D. degree from Caltech in 2006. She was a Humboldt postdoctoral fellow at the Max-Planck-Institute for Bioinorganic Chemistry. In 2009, she began independent research at the University of Minnesota, where she is currently an Associate Professor of Chemistry. Her research interests include metal-metal bonding, activation of small-molecules, electronic structure, and catalysis. She is a member of the Editorial Advisory Boards of Inorganic Chemistry and Chemical Society Reviews.

Learn more about Dr. Lu and her research group here.

 

Steven Mansoorabadi

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Steven Mansoorabadi

Assistant Professor of Chemistry and Biochemistry
Auburn University

 Steven Mansoorabadi

Dr. Mansoorabadi recieved his Ph.D. in Biochemistry from the University of Wisconsin-Madison under the supervision of Professor George H. Reed.  He then performed his post-doctoral studies in the laboratory of Professor Hung-Wen (Ben) Liu at the Univeristy of Texas at Austin.  Dr. Mansoorabadi joined the faculty of Auburn University in 2012.

Learn more about Dr. Mansoorabadi here.

Michael Marletta

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Michael Marletta

Professor of Chemistry
Professor of Molecular and Cell Biology
CH and Annie Li Chair in the Molecular Biology of Diseases
University of California, Berkeley

 Michael Marletta

Michael A. Marletta was born in Rochester New York on February 12, 1951. He graduated from the Aquinas Institute in 1969. After an A.B. degree in biology and chemistry from Fredonia, State University of New York (1973), he received a PhD in 1978 from UCSF with George L. Kenyon followed by a 2-year postdoctoral appointment at MIT with Christopher Walsh.

 

In 1980 was appointed Assistant Professor in the Department of Applied Biological Sciences and was promoted to Associate Professor in 1986 at MIT. In 1987 he moved to the University of Michigan as Associate Professor of Medicinal Chemistry and Associate Professor of Biological Chemistry. In 1991 he was promoted to Professor and appointed the John G. Searle Professor of Medicinal Chemistry. In 1997 he became an Investigator in the Howard Hughes Medical Institute. Marletta moved to the University of California, Berkeley in 2001 as Professor of Chemistry, Department of Chemistry and Professor of Biochemistry, Department of Molecular and Cell Biology. He was appointed the Aldo DeBenedictis Distinguished Professor of Chemistry in 2002. He served as Chair of the Department of Chemistry at Berkeley from 2005-2010. In July 2011 he joined the faculty of The Scripps Research Institute, served as President and CEO, and then returned to his present position in Berkeley in 2015.

 

Awards he has received include the George H. Hitchings Award for Innovative Methods in Drug Discovery and Design (1991) sponsored by the Burroughs Welcome Fund; Faculty Recognition Award from Michigan (1992); Outstanding Alumni Achievement Award from SUNY Fredonia (1993); MacArthur Fellowship awarded by the John D. and Catherine

T. MacArthur Foundation (1995); elected Senior Fellow in the Michigan Society of Fellows and elected to the SUNY Honor Role (1996); elected to the Institute of Medicine (now the National Academy of Medicine) (1999); Distinguished Faculty Lectureship Award in Biomedical Research University of Michigan Medical School (2000). In 2000 he was selected for Distinguished Faculty Achievement Award at Michigan. In 2001 he was elected to the American Academy of Arts and Sciences and also a fellow of the AAAS. He was elected to the National Academy of Sciences in 2006. He was elected a Fellow of the Royal Society of Chemistry in 2009. He was elected to the American Philosophical Society in 2016. He received the Harrison Howe Award (2004) of the American Chemical Society, and in 2007 the Repligen Award, Biological Chemistry Division of the American Chemical Society and the Kaiser Award from the Protein Society and the Esselen Award for Chemistry in the Public Interest, Northeastern Section of the American Chemical Society, the Murray Goodman Memorial Prize (2009), and the Alfred Bader Award for Bioinorganic or Bioorganic Chemistry (2015). In 2014 he received the American Association of State Colleges and Universities AASCU Distinguished Alumnus Award. He will be awarded a Doctor of Science honorary degree by SUNY in 2018.

 

He is a member of the American Chemical Society and the American Society for Biochemistry and Molecular Biology. He serves on the editorial board of PNAS, Biochemistry and eLife. He is a consultant for a number of pharmaceutical companies and serves on the scientific advisory boards of several others including Cayman Chemical. He is a co- founder of Omniox, Inc. He is a member of the Fredonia College Foundation Board of Directors and chair of Science Advisory Council at Fredonia. He also serves on the advisory board of a number of university departments and centers.

 

Marletta's primary research interests lie at the interface of chemistry and biology with emphasis on the study of protein function and enzyme reaction mechanisms. Marletta has made fundamental discoveries concerning the biological action of nitric oxide. His studies have provided the basis for understanding at the molecular level of this unique cell signaling pathway and the function of nitric oxide in the immune system. He has uncovered several novel structure/function relationships in nitric oxide synthase and guanylate cyclase. His continued studies on NO signaling have recent led to a molecular understanding of general gas sensing mechanisms in biology. A new research direction involves novel oxidative enzymology of cellulose degradation with application to biofuel production.

 

Marletta is married to Margaret Gutowski and they have a son Matthew.

 
Learn more about Dr. Marletta here.

Learn more about the Marletta Laboratory here.

Sabeeha Merchant

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Sabeeha Merchant

Distinguished Professor of Chemistry and Biochemistry
UCLA

 Sabeeha Merchant

Sabeeha Merchant is Director of the Institute for Genomics and Proteomics and Distinguished Professor of Chemistry and Biochemistry at UCLA. She earned degrees in Molecular Biology and Biochemistry from the University of Wisconsin, Madison, and undertook post-doctoral studies at Harvard University prior to her professorial appointment. Merchant’s discoveries have influenced scholarly thought in diverse disciplines, from biogeochemistry and biological oceanography to photosynthesis, plant biochemistry and human nutrition. Merchant formulated the concepts of elemental sparing and recycling, which operate to sustain life in situations of deficiency by prioritized distribution of the limiting resource. Her concept of “reduce and re-use” has now been demonstrated across the kingdom of life. Merchant is recognized separately in plant biology for discoveries relating to chloroplast biogenesis and contributions to the genomics of algae. Merchant has served on advisory boards in government, academia and industry and is presently Editor of the Annual Reviews of Plant Biology and Editor-in-Chief of The Plant Cell. Her accomplishments are recognized by a Guggenheim fellowship, major awards from the American Society of Plant Biologists, the National Academy of Sciences and the Alexander von Humboldt Foundation, and election to the National Academy of Sciences, the American Academy of Arts and Sciences and the Leopoldina.

Learn more about Dr. Merchant and her group here

Frank Neese

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Frank Neese

Director
The Max Planck-Institut für Kohlenforschung

Frank Neese

Frank Neese received both his Diploma (Biology – 1993) and Ph.D (Dr. rer. Nat. – 1997) working with Prof. P. Kroneck at the University of Konstanz. He performed postdoctoral work at Stanford University with Prof. E. I. Solomon from 1997 to 1999, then returned to Konstanz where he completed his habilitation in 2001. He joined the Max Planck Institute (MPI) for Bioinorganic Chemistry in 2001 as a group leader, where he directed a research group until accepting the position of full Professor and Chair of Theoretical Chemistry at the University of Bonn in 2006. In 2008, Neese returned part time to the MPI as one of its rare “Max Planck Fellows” within the Department of Inorganic Chemistry. In 2011, he became Director of the MPI for Bioinorganic Chemistry, renamed in 2012 in MPI for Chemical Energy Conversion, where he heads the department of Molecular Theory and Spectroscopy. In 2005, Neese received the Hellmann Award of the German Theoretical Chemical Society for the Development and Application of new Theoretical Methods and subsequently the Klung-Wilhelmy Weberbank Award in 2008 and the Gottfried Wilhelm Leibniz Award of the German Science Foundation in 2010. In 2013, he was inducted into the Leopoldina Nationale Akademie der Wissenschaften (German National Academy of Sciences). He was Associate Editor (2011-2014) of the journal PhysChemChemPhys and is a Member of the International Academy of Quantum Molecular Sciences (IAQMS, since 2012). Since 2015 Frank Neese is Associate Editor of the journal Inorg. Chem. and as of 2016 he is Member of the Editorial Board of the review book series Struct. Bond.. As of 2016 Neese has been appointed as an active member of the International Advisory Board for the Institute of Organic Chemistry and Biochemistry (IOCB) of the Czech Academy of Sciences in Prague and he was elected as a new Member of the Review Board „Physical and Theoretical Chemistry“ in the field of „General Theoretical Chemistry“ of the Deutsche Forschungsgemeinschaft (German Research Foundation, DFG). Frank Neese is the author of more than 440 scientific articles in journals of Chemistry, Biochemistry and Physics. His work focuses on the Theory of Magnetic Spectroscopies (electron paramagnetic resonance, magnetic circular dichroism) and their experimental and theoretical application, local pair natural orbital correlation theories, spectroscopy oriented configuration interaction, electronic and geometric structure and reactivity of transition metal complexes and metalloenzymes. He is lead author of the ORCA program.

Learn more about The Max Planck Institut für Kohlenforschung here.

Nigel Robinson

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Nigel Robinson

Professor of Biology
Durham University

 Nigel Robinson

About a half of the reactions of life require metals and Nigel Robinson has contributed towards understanding how living cells help to direct these vital inorganic elements to the correct protein locations.  He has studied the cell biology of metals for more than three decades, mostly in microbes and plants, and co-established (with Dennis Winge, Utah) the Gordon Research Conference series on the Cell Biology of Metals. He directs the BBSRC Network in Industrial Biotechnology and Bioenergy (IBBE) on “Metals in Biology: Elements of IBBE”. Robinson’s group cloned the ferric-chelate reductases needed for iron-uptake by plants (non-grass species) (Nature 1999 397: 694-697). Using bacterial models he found that two enzymes with similar metal-binding sites, similar cupin-folds and similar metal-affinities acquire different metals, copper and manganese, by folding in different cellular compartments (Nature 2008 455: 1138-1142). These observations demonstrate that metal availability at the site of protein folding dominates metal-protein speciation in vivo. His research group characterised multiple components of the cellular machinery that sustains these vital metal-availabilities including DNA-binding, metal-sensors (reviewed in Nature 2009 460: 823-830), metal storage-proteins (PNAS 2001 98: 9593-9598), and copper metallochaperones engaged in metal-delivery (PNAS 2012 109: 95-100; reviewed in Ann Rev Biochem 2010 79: 537-562). The group recently discovered that the set point of a metal sensor is tightly-tuned to, but does not govern, the buffered intracellular concentration of its cognate metal (Nature Chemical Biology 2017 13: 409-414), providing a “window” through which the free energies of metals can be viewed inside cells.

Learn more about Dr. Robinson  here.

Amy Rosenzweig

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Amy Rosenzweig

Weinberg Family Distinguished Professor of Life Sciences
Professor of Molecular Biosciences and Chemistry
Northwestern University

 Amy Rosenzweig

Amy C. Rosenzweig, a native of Pittsburgh, PA, recieved a B.A. in chemistry from Amherst College, a Ph.D. in inorganic chemistry from Massachusetts Institute of Technology, and conducted postdoctoral research at Harvard Medical School.  She is a fellow of the American Academy of Arts and Sciences (2014) and a member of the National Academy of Sciences (2017).  Her awards include the Royal Society of Chemistry Joseph Chatt Award (2014), the American Chemical Society Nobel Laureate Signature Award for Graduate Education (2006), an Honorary Doctor of Science Degree from Amherst College (2005), and a MacArthur Fellowship (2003).

Learn more about the Rosenweig Lab here.

Daniel Rothman

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Daniel Rothman

Professor of Geophysics
Massachusetts Institute of Technology

 Daniel Rothman

Daniel H. Rothman is a Professor of Geophysics in the Department of Earth, Atmospheric, and Planetary Sciences at MIT.  His work has contributed widely to the understanding of the organization of the natural environment, resulting in fundamental advances in subjects ranging from seismology and fluid flow to biogeochemistry and geobiology.  He has also made significant contributions to research in statistical physics.  Much of his recent interests focus on the dynamics of Earth's carbon cycle, the co-evolution of life and the environment, and the physical foundation of natural geometric forms.

Rothman joined the MIT faculty in 1986, after receiving his AB in applied mathematics from Brown University and his PhD in geophysics from Stanford University. He has held visiting appointments at the University of Chicago, Ecole Normale Superieure, and Harvard's Radcliffe Institute for Advanced Study, and has been honored as a Fellow of the American Physical Society and the American Geophysical Union.  He is the recipient of the 2016  Levi L. Conant Prize from the American Mathematical Society

Rothman is co-founder and co-director of MIT's Lorenz Center, a privately funded interdisciplinary research center devoted to learning how climate works. The Science Philanthropy Alliance recently issued a proposal by Rothman and a group of his colleagues for a major new research initiative on mass extinction and Earth-system stability.

Learn more about the Rothman Group here.

Lance Seefeldt

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Lance Seefeldt

Professor of Chemistry and Biochemistry
Utah State University

 Lance Seefeldt

Lance Seefeldt is a Professor of Chemistry and Biochemistry at Utah State University.  His research seeks to gain insights into the mechanism of the metalloenzyme nitrogenase.  To acheive this goal, a wide range of methods are utilized.

Learn more about Dr. Seefeldt and his research here.

Mohammed Seyedsayamdost

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Mohammed Seyedsayamdost

Assisant Professor of Chemistry & Molecular Biology
Princeton University

Mohammed Seyedsayamdost

Mo was born in Iran and grew up in Germany and Australia before entering Brandeis University (Waltham, MA) for his undergraduate studies. There he obtained a 4-year combined B.S./M.S. degree in Biochemistry with highest honors. His undergraduate thesis was carried out in the laboratory of Prof. Lizbeth Hedstrom on the chemical mechanism of inosine-5′-monophosphate dehydrogenase, an important target of immunosuppressive drugs. Mo carried out his graduate studies in the Department of Chemistry at MIT under the guidance of Prof. JoAnne Stubbe. His PhD thesis combined methods for site-specific incorporation of unnatural amino acids with rapid kinetic and spectroscopic techniques in order to examine the mechanism of ribonucleotide reductase, an essential metalloenzyme in all living cells. These studies revealed an unprecedented pathway and mechanism for long-range proton-coupled electron transfer catalyzed by transient amino acid radicals. He then joined the labs of Prof. Jon Clardy and Prof. Roberto Kolter as a Novartis LSRF postdoctoral fellow at Harvard Medical School, where he examined the roles of small molecules in mediating microbial interspecies interactions. This work led to the discovery of a novel family of phytotoxins as well as to new approaches for prospecting for bioactive small molecules. In January 2013, Mo started as an assistant professor in the Department of Chemistry at Princeton University. His lab is interested in the discovery, structure, function, and biosynthesis of new small molecules with bioactive or therapeutic properties. These studies blend approaches from microbiology, bacterial genetics, small molecule chemistry, biochemistry, and mechanistic enzymology.

 

Mo has been the recipient of the Novartis Life Sciences Research Foundation Fellowship, the NIH Pathway to Independence Award (K99/R00), the Searle Scholars Award, the Pew Biomedical Scholars Awards, co-recipient of the Princeton Environmental Institute’s Innovative Research Award, and the NIH Director’s New Innovator Award.

 

Learn more about The Seyedsayamdost Research Group here.

Joanne Stubbe

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Joanne Stubbe

Novartis Professor of Çhemistry emeritus
Massachussetts Institute of Technology

 Joanne Stubbe

One of Dr. Stubbe's major contributions has been to our understanding of the free radical chemistry of ribonucleotide reductases (RNRs), enzymes essential in the transformation of RNA building blocks to DNA building blocks.  These enzymes provide the dNTPs required for DNA replication and repair and play and essential role in the fidelity of these processes.  Dr. Stubbe has identified the importance of three unique types of thiyl-radicals in the nucleotide reduction process itself.  Her studies have led to the design of a mechanism-based inhibitor gemcitabine, currently used clinically.  We have elucidated an unprecedented 35 A oxidation by the stable tyrosyl radical in one subunit of RNR of a cysteine to a thiyl radical in the active site of the second subunit.  The oxidation involves multiple proton coupled electron transfer steps and three transient tryosyl radical intermediates.  Dr. Stubbe has elucidated the mechanism of biosynthesis and repair of the unprecedented diferric-tyrosyl radical cofactor essential for all class I RNR catalysis.

In 2010 Dr. Stubbe identified the first, dimanganese-tyrosyl radical cofactor in the class Ib RNRs.  These cofactors, distinct from the diferric-tyrosyl radical cofactors in human RNR, are likely unique to many pathogenenic organisms.  Dr. Stubbe has elucidated the biosynthetic pathways of this cluster that represents a new target from antibacterial therapeutics.   Most recently, Dr. Stubbe's focus has turned to the quaternary structure complexity of RNRs and its alteration by the clinically unsed drugs gemcitabine and clofarabine.

 

 

Kenichi Yokoyama

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Kenichi Yokoyama

Assistant Professor of Biochemistry
Duke University Medical Center

 Kenichi Yokoyama

Dr. Yokoyama’s group has been studying biosynthesis and mechanism of actions of medicinally important cofactors and natural products. One of our focus is C-C bond forming radical SAM enzymes critical for the formation of the carbon skeletons of the metabolites. Our studies are revealing the mechanisms of enzymes, in which highly reactive free radicals are used to construct structurally complex metabolites.

Learn more about the Yokoyama Lab here.