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37th Summer Symposium Speakers

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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.

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