DOCSLIB.ORG

Frank Neese: "Combined Experimental and Theoretical

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Frank Neese: TInC 2014 – Bioinorganic Chemistry May 22 at Medicon Village, Lund Programme 08.30‐09.00 Registration 09.00‐09.05 Welcome 09.05‐10.00 Artificial metalloenzymes: challenges and opportunities Thomas R Ward, Department of Chemistry, University of Basel, Switzerland http://www.chemie.unibas.ch/~ward/ 10.00‐10.30 Coffee break 10.30‐11.30 Combined experimental and theoretical studies on the active site of nitrogenase Frank Neese, Max‐Planck Institute for Chemical Energy Conversion, Germany www.cec.mpg.de/menschen/direktoren/frank‐neese/vita.html 11.30‐12.30 Photoactivated and organometallic anticancer complexes Peter Sadler, Department of Chemistry, University of Warwick, UK http://www2.warwick.ac.uk/fac/sci/chemistry/research/sadler/ 12.30‐14.00 Lunch (Lunch may be purchased for 75 SEK at Medicon Village. There are also several other lunch restaurants in the immediate vicinity) 14.00‐15.00 Copper/dioxygen bioinorganic chemistry Edward Solomon, Department of Chemistry, Stanford University, USA www.stanford.edu/group/solomon/home.html 15.00‐15.30 Coffee break 15.30‐16.30 Title to be announced Amy Rosenzweig, Department of Molecular Biosciences, Northwestern University, USA http://groups.molbiosci.northwestern.edu/rosenzweig/ 16.30‐17.30 The amazing high‐valent iron‐oxo reaction landscape Lawrence Que, Department of Chemistry, University of Minnesota, USA http://bioinorg.chem.umn.edu/quespace/ 17.30‐18.30 Poster session 18.30‐ Dinner (Optional in registration form for 375 SEK incl moms/VAT) TInC 2014 – Bioinorganic Chemistry May 22 at Medicon Village, Lund Poster Abstracts NOTE! Please put your poster on the board with your poster number on. The poster number (PN) is the same as the page number in this document. List of Abstracts Nr. Title Presenting Author 1. Synthesis and properties of new biomimetic [2Fe-2S] clusters Marie Bergner 2. Bulky N,N,O ligands in mononuclear non-Heme iron enzyme mimics Emma Folkertsma 3. Iron(II)- and oxoiron(IV)-tetracarbenes – reactivity towards small molecules and more Claudia Kupper 4. Electronics study on the hydroxo-bridged diiron(III) bisporphyrin systems Mala A. Sainna 5. Halogen-bonding stabilizes a Fe(III)-oxo transfer reagent adduct Christine J. McKenzie 6. Reactions of Rieske-type biomimetic [2Fe–2S] clusters with nitric oxide Christine Schiewer 7. New pyrazolate based diiron complexes for the activation of dioxygen and for water oxidation Anne Schober 8. Design and synthesis of bioinspired iron complexes with dinucleating polydentate ligand Albert A. Shteinman 9. Gas phase chemistry of [LFeO]+ complexes Simon Svane 10. From model complexes of Tyrosinase and its inhibited forms to the design and study of new inhibitors Elina Buitragoa 11. Mimicking copper mediated dioxygen activation with the assistance of BOX ligands: A switch from μ-η2:η2-peroxo to bis(μ-oxo) dicopper(II) core by virtue of a base Vandana E. Goswami 12. Dioxygen activation studies with a bio-inspired copper complex Nicole Kindermann 13. Hybrid QM/QM studies of molybdenum enzymes –Reaction pathways and redox potentials Milica Andrejić 14. Synthesis of pyrazine-pyrane-dithiolene ligands mimicing specific features of molybdopterin Claudia Schindler 15. Pyrazolbased ligand scaffolds provide second sphere hydrogen bonding: substrate coordination by bimetallic complexes Natascha Bruckner 16. Manganese complexes of monocarboxylato ligands as catalysts for epoxidation Claire Deville 17. Chromium(V)-oxo and chromium(IV)-O2 adducts derived from an unusually labile chromium(III) complex David P. De Sousa 18. Development of new vanadium (IV/V) catalysts with non-innocent ligands for the enantioselective oxidation of prochiral sulfides Lina Fischer 19. Photosystem II like water oxidation mechanism in a bioinspired tetranuclear manganese complex Rong-Zhen Liao 20. Thymol bromination: a comparison between enzymatic and chemical catalysis Federica Sabuzi 21. Insight into the reaction of novel ruthenium based water oxidation catalysts Thorsten Stolper 22. Crystals that breathe Jonas Sundberg 23. Fatty acid oxidizing enzymes in Lobosphera incise Benjamin Djian 24. Synthesis and application of modified and labelled lipids C. Hansen 25. Reversible conversion of formate and CO2 by formate dehydrogenase from Rhodobacter capsulatus Tobias Hartmann 26. Studies on the active site of E. coli TMAO reductase using a defined in vitro assay for the reconstitution of apo-TMAO reductase activity with bis-MGD Paul Kaufmann 27. Structural basis for the formation of a bis-allylic hydroperoxide by a cyanobacterial lipoxygenase Julia Newie 28. Combinatorial nucleotide deletion analysis of functional nucleic acids Katarzyna Wawrzyniak-Turek 29. Uptake of essential metal ions mediated by periplasmic binding proteins Ellis Wilde 30. Functional characterization of a dodecaheme c-type cytochrome involved in microbial electron transfer to energy production in MFCs Mónica N. Alves 31. Cytochrome P450 enzymes are valuable biocatalysts Viktoria Bruckhoff 32. Arsenic resistance and detection of arsenic reduction and oxidation abilities of bacterial strains isolated from contaminated soil Marek Chyc 33. Effect of selected types of soot on germination, growth and some physiological parameters of Arabidopsis thaliana Marek Chyc 34. DF-Click: a modular approach to the de novo design of metalloprotein catalysts M. Chino 35. Using modified zinc finger domains as selective DNA hydrolysis tool or fluorescence metal probe F. Czerny 36. Transition metal-binding G-quadruplexes David M. Engelhard 37. Rigid spin labels for studies of RNA secondary structures Anne Ochmann 38. Interfering with RNAi; a study of platination and abasic sites modifications of miR-146a Alak Alshiekh 39. Towards metal-mediated DNA nanostructures containing a trans-chelating ligand Fernanda A. Pereira 40. Specific interactions of synthetic metallopeptides with target DNA H. Rao 41. Modified nucleotides as fluorescent probes and for the investigation of the orotidine decarboxylase mechanism Julia Schneider 42. Tetrazole-based gold(I) complexes as a new group of anticancer agents Tatiyana Serebryanskaya 43. The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor Nadine Böhmer 44. Bispidine iron(IV)-oxo complexes: kinetics and electronic properties Anna-Maria Rensland 45. A mononuclear iron(III)-peroxide that breaks strong C-H bonds with high reaction rates Joan Serrano .
Load more

Recommended publications
  • Dioxygen Activation in Soluble Methane Monooxygenase
    Dioxygen Activation in Soluble Methane Monooxygenase The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Tinberg, Christine E., and Stephen J. Lippard. “Dioxygen Activation in Soluble Methane Monooxygenase.” Accounts of Chemical Research 44.4 (2011): 280–288. As Published http://dx.doi.org/10.1021/ar1001473 Publisher American Chemical Society Version Author's final manuscript Citable link http://hdl.handle.net/1721.1/69856 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. Dioxygen Activation in Soluble Methane Monooxygenase† Christine E. Tinberg and Stephen J. Lippard* Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139 RECEIVED DATE (to be automatically inserted after your manuscript is accepted if required according to the journal that you are submitting your paper to) * To whom correspondence should be addressed. E-mail: [email protected]. Telephone: (617) 253-1892. Fax: (617) 258-8150. †Work from our laboratory discussed in this Account was funded by grant GM032134 from the National Institute of General Medical Sciences. 1 CONSPECTUS The controlled oxidation of methane to methanol is a chemical transformation of great industrial importance that is underutilized because of inefficient and costly synthetic procedures. Methane monooxygenase enzymes (MMOs) from methanotrophic bacteria achieve this chemistry efficiently under ambient conditions. In this Account we discuss the first step in the oxidation of methane at the carboxylate-bridged diiron active site of the soluble MMO (sMMO), namely, the reductive activation of atmospheric O2.
    [Show full text]
  • The Life of a Professor Email Print
    Log In ACS ACS Publications C&EN CAS About Subscribe Advertise Contact Join ACS Serving The Chemical, Life Sciences & Laboratory Worlds Search Adv anced Search Home Magazine News Departments Collections Blogs Multimedia Jobs Home > Volume 92 Issue 11 > The Lif e Of A Prof essor Volume 92 Issue 11 | pp. 14-18 Issue Date: March 17, 2014 0 0 MOST POPULAR COVER STORIES: TRAILBLAZER AND MENTOR Viewed Commented Shared The Life Of A Professor Email Print Spider Silk Poised For Commercial Department: Science & Technology, ACS News | Collection: Life Sciences Entry News Channels: JACS In C&EN Keywords: Priestley Medal, Stephen Lippard Controversy Clouds E-Cigarettes Reports Make Progress In Transforming C–H Bonds Into Druglike Motifs I am honored to receive the 2014 Priestley Medal. The award is a tribute to the talented Cover Stories students, both graduate and undergraduate, as well as postdoctoral associates who Global Top 50 have trained with me over nearly 50 years. I am proud of these individuals, for their Trailblazer And Mentor Milk Proteins Protect Fabrics From courage in agreeing to venture onto new snowfields to place the first footprints, for their The Life Of A Professor Fire relentless pursuit of the truth, and for their creative ideas and clever experiments that *Most Viewed in the last 7 days brought insight where previously there was often confusion. Of equal importance are the many collaborators who have greatly facilitated our ability to Advertisement make progress in areas beyond our knowledge base. If “professor” stands for “professional student,” these individuals have been my teachers. I thank them, the ACS Board of Directors who award this medal, and those who entered and supported my nomination.
    [Show full text]
  • Nitrosocyanin, a Red Cupredoxin-Like Protein from Nitrosomonas Europaea† David M
    © Copyright 2002 by the American Chemical Society Volume 41, Number 6 February 12, 2002 Accelerated Publications Nitrosocyanin, a Red Cupredoxin-like Protein from Nitrosomonas europaea† David M. Arciero,‡ Brad S. Pierce,§ Michael P. Hendrich,§ and Alan B. Hooper*,‡ Department of Biochemistry, Molecular Biology and Biophysics, UniVersity of Minnesota, St. Paul, Minnesota 55108, and Department of Chemistry, Carnegie Mellon UniVersity, Pittsburgh, PennsylVania 15213 ReceiVed NoVember 1, 2001; ReVised Manuscript ReceiVed December 20, 2001 ABSTRACT: Nitrosocyanin (NC), a soluble, red Cu protein isolated from the ammonia-oxidizing autotrophic bacterium Nitrosomonas europaea, is shown to be a homo-oligomer of 12 kDa Cu-containing monomers. Oligonucleotides based on the amino acid sequence of the N-terminus and of the C-terminal tryptic peptide were used to sequence the gene by PCR. The translated protein sequence was significantly homologous with the mononuclear cupredoxins such as plastocyanin, azurin, or rusticyanin, the type 1 copper-binding region of nitrite reductase, and the binuclear CuA binding region of N2O reductase or cytochrome oxidase. The gene for NC contains a leader sequence indicating a periplasmic location. Optical bands for the red Cu center at 280, 390, 500, and 720 nm have extinction coefficients of 13.9, 7.0, 2.2, and 0.9 mM-1, respectively. The reduction potential of NC (85 mV vs SHE) is much lower than those for known cupredoxins. Sequence alignments with homologous blue copper proteins suggested copper ligation by Cys95, His98, His103, and Glu60. Ligation by these residues (and a water), a trimeric protein structure, and a cupredoxin â-barrel fold have been established by X-ray crystallography of the protein [Lieberman, R.
    [Show full text]
  • 2018 FACULTY RECOGNITION DINNER the Honorees
    The 31st Annual FACULTY RECOGNITION DINNER Kellogg Global Hub October 25, 2018 The 31st Annual FACULTY RECOGNITION DINNER is hosted by President Morton Schapiro and Provost Jonathan Holloway. It honors members of the Northwestern faculty who have brought distinction to the University by earning important external recognition in the past year. The multidisciplinary Faculty Honors Committee reviewed award recipients identified by the deans and department chairs, selecting the most prestigious awards for University recognition. Each subcommittee reviewed awards in its respective fields. Arts and Humanities Life and Medical Chris Abani Sciences Richard Kieckhefer Serdar Bulun Sara Maza Bob Lamb Saul Morson Amy Rosenzweig Natasha Trethewey Clyde Yancy Engineering and Physical Social Sciences Sciences David Austen-Smith Yonggang Huang Shari Diamond Bryna Kra Jamie Druckman Tobin Marks Jan Eberly Chad Mirkin Larry Hedges Greg Olson Joel Mokyr Monica Olvera de la Cruz John Rogers Richard Silverman The Honorees Jan Achenbach Zdeněk Bažant Honorary Doctor of Science ASME Medal Clarkson University American Society of Mechanical Engineers Emma Adam Foreign Member Lyle Spencer Research Award Academy of Athens Spencer Foundation Alfred M. Freudenthal Medal Erik Andersen American Society of Civil Engineers Faculty Early Career Development (CAREER) Award Karl Bilimoria National Science Foundation President Association for Academic Surgery Torben Andersen Fellow Michelle Birkett Society for Economic Measurement Inaugural Member National Academies of Sciences,
    [Show full text]
  • “Metalloproteins at the Crossroads of Design & Nature”
    Virtual Symposium “Metalloproteins at the crossroads of design & nature” 27 January 2021 Keynote Lecture Prof. Hannah Shafaat Ohio State University Emergent Complexity: Reconstructing primordial energy conversion processes in model metalloproteins Abstract: Nature has evolved diverse systems to carry out energy conversion reactions. Metalloenzymes such as hydrogenase, carbon monoxide dehydrogenase, acetyl coenzyme A synthase, and methyl coenzyme M reductase use earth- abundant transition metals such as nickel and iron to generate and oxidize small-molecule fuels such as hydrogen, carbon monoxide, acetate, thioesters, and methane. These reactions are highly valuable to understand and harness in the context of the impending global energy and climate crisis. However, the native enzymes require complex multimetallic cofactors, are costly to isolate, highly sensitive to external conditions, and generally poorly suited for large- scale application. We are applying metalloprotein engineering approaches in order to better understand the mechanisms of the native enzymes and develop robust functional models with potential for implementation in anthropogenic energy conversion. Robust metalloprotein scaffolds such as rubredoxin, ferredoxin, and azurin and have been converted into model systems that mimic the structure and function of complex nickel metalloenzymes. By introducing non-native metals and redesigning the primary and secondary coordination spheres, we have installed novel activity into these simple electron transfer proteins, including
    [Show full text]
  • Two Coppers Are for Methane Oxidation** Richard A
    Highlights DOI: 10.1002/anie.201003403 Methane Monooxygenase One is Lonely and Three is a Crowd: Two Coppers Are for Methane Oxidation** Richard A. Himes, Kevin Barnese, and Kenneth D. Karlin* binuclear complexes · bioinorganic chemistry · copper · methane monooxygenase · oxidation Mild activation of inert CÀH bonds attracts increasingly and catalytic reactivity,[2b] 2) a diiron active site,[4] and 3) a feverish research efforts as the global predicament of dwin- dicopper center. dling resources grows increasingly dire. The desirability of That last proposal rose to the forefront with the publica- methane as a chemical feedstock presents itself in this tion of the enzymes first X-ray crystal structure (Figure 1).[5] context: Functionalization of this simplest hydrocarbon Although a major breakthrough, this fruit of Rosenzweig and would unlock the worlds reserves of natural gas for the synthesis of necessary chemicals from this abundant C1 building block. However, with a CÀH bond strength of 104 kcalmolÀ1, methane possesses the most difficult hydro- carbon bond to oxidize. Current industrial methods for converting methane into useful chemical products incur prohibitive energy costs and lack selectivity.[1] Not so for natures methane monoxygenases, the enzymes utilized in the metabolism of CH4 by bacteria that use methane as a primary energy and biosynthetic material source. Two enzyme classes, soluble methane monooxygenase (sMMO) and particulate methane monooxygenase (pMMO), selectively oxidize CH4 to CH3OH at ambient temperature and pressure. The well-understood sMMO employs an active- site diiron cluster to bind and activate dioxygen for this two- electron oxidation. Extensive bioinorganic research over several decades has successfully elucidated the probable mechanistic pathways for sMMO catalysis.[2] By contrast, the transmembrane protein pMMO has been recalcitrant in yielding the secrets of its structure and reactivity.
    [Show full text]
  • The Rise of Radicals in Bioinorganic Chemistry
    HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Isr J Chem Manuscript Author . Author manuscript; Manuscript Author available in PMC 2017 October 01. Published in final edited form as: Isr J Chem. 2016 October ; 56(9-10): 640–648. doi:10.1002/ijch.201600069. The Rise of Radicals in Bioinorganic Chemistry Harry B. Gray and Jay R. Winkler Beckman Institute, California Institute of Technology, 1200 E California Boulevard, Pasadena, CA 91125, USA Abstract Prior to 1950, the consensus was that biological transformations occurred in two-electron steps, thereby avoiding the generation of free radicals. Dramatic advances in spectroscopy, biochemistry, and molecular biology have led to the realization that protein-based radicals participate in a vast array of vital biological mechanisms. Redox processes involving high-potential intermediates formed in reactions with O2 are particularly susceptible to radical formation. Clusters of tyrosine (Tyr) and tryptophan (Trp) residues have been found in many O2-reactive enzymes, raising the possibility that they play an antioxidant protective role. In blue copper proteins with plastocyanin- like domains, Tyr/Trp clusters are uncommon in the low-potential single-domain electron-transfer proteins and in the two-domain copper nitrite reductases. The two-domain muticopper oxidases, however, exhibit clusters of Tyr and Trp residues near the trinuclear copper active site where O2 is reduced. These clusters may play a protective role to ensure that reactive oxygen species are not liberated during O2 reduction. Keywords Electron transfer; radicals; tyrosine; tryptophan Introduction Arguably the most important chemical reaction on our planet is water oxidation to oxygen in green plants.
    [Show full text]
  • 10Th International Copper Research Meeting (Copper 2016 Sorrento)
    10th International Copper Research Meeting (Copper 2016 Sorrento) Organizers: Stephen G. Kaler, Scot C. Leary, and Roman S. Polishchuk. Post-Conference Report The 10th International Copper Research Meeting (Copper 2016) was held at the picturesque seaside town of Sorrento in Italy, running from 25-30th Sept. The meeting is held every two years, usually in a similar southern Italian coastal city and attracts researchers interested in copper across broad fields of science. This year was no exception with a strong attendance of 127 delegates with a strong representation of clinical researchers in addition to many scientists in fundamental areas including microbial, plant, human health and medicine, neuroscience, cell biology, cancer and protein structure. The location was at the Grand Hotel Vesuvio, perched up in the hills with great views overlooking Sorrento and across to Mount Vesuvius. The location was ideal and provided excellent support for the meeting. Attendance: Attendees represented many nations including Argentina, Australia, Brazil, Canada, Italy and many European Union countries, Japan, United Kingdom, and USA. The conference also received strong support from the Royal Society of Chemistry journal, Metallomics with a dedicated special issue on copper research linked to the meeting (Mammalian Copper Transport and Related Disorders) and support of the best poster awards. In addition to an exciting line-up of plenary and symposia sessions, there was a strong showing of support for posters with ~50 posters and a session dedicated to oral presentations from selected poster presenters. Two poster sessions were well-attended with active scientific discussions continuing from the sessions into dinner. Importantly, there was good attendance from new delegates, and plenty of young researchers, demonstrating the continued strength and strong future for the copper research community.
    [Show full text]
  • March 2019 NUCLEUS 2-22-19Web
    DED UN 18 O 98 F http://www.nesacs.org N Y O T R E I T H C E N O A E S S S L T A E A C R C I N S M S E E H C C TI N O CA March 2019 Vol. XCVII, No.7 N • AMERI Monthly Meeting 2018 Richards Award to Chad A. Mirkin at Harvard Who Was Theodore William Richards? By M. S. Simon Volunteering with the United States Pharmacopeia By Chris Moreton Carolyn R. Bertozzi to Receive 2019 Esselen Award rings of Saturn through a four-inch tele- and precise. Hence, in trying to satisfy Who was scope by Professor Josiah Parsons a desire which had as its object the dis- Cooke, Jr. of Harvard while the family covery of more knowledge concerning Theodore was at Newport, R.I. the fundamental nature of things, one At ten he was making Pharaoh’s naturally assigns to the atomic weights Serpents with mercuric thiocyanate and an important place.” William coloring flames with various salts. He In the following years Richards and obtained money to set up a chemistry his students (if we include independent Richards? laboratory when he was 13 by printing work of Baxter and Hönigschmid, who on a hand press, copywriting, and sell- had been trained by him) determined the by M.S. Simon ing an edition of his mother’s sonnets. atomic weight of 55 of the 92 known el- Adapted from The NUCLEUS, 1996 (3) He was allowed to attend chemistry ements, in many cases in parts per ten 4 ff lectures at the University of Pennsylva- thousand, in some, parts per hundred nia, and at 14 entered and studied chem- thousand.
    [Show full text]
  • Mechanistic and Physical Studies of Methane Monooxygenase from Methylococcuscapsulatus (Bath)
    2, Mechanistic and Physical Studies of Methane Monooxygenase from Methylococcuscapsulatus (Bath) by Katherine E. Liu B.A., Cornell University (1989) Submitted to the Department of Chemistry in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy at the Massachusetts Institute of Technology February, 1995 © 1995 Massachusetts Institute of Technology All rights reserved Signature of Author Department of Chemistry November 14, 1994 Certified by -- -- -- V U I/ Professor Stephen J. Lippard Thesis Supervisor /q~ Accepted by Professor Dietmar Seyferth Chairman, Departmental Committee on Graduate Students e-;.{ence . : -. .; 1QO D 2 This doctoral thesis has been examined by a Committee of the Department of Chemistry as follows: Professor Alan Davison, Committee Chair /'-- l' 6/O ProfessorStephen J. Lippard Arthur Amos Noyes Professor of Chemistry PA fessor JoAnne Stubbe John G. Sheehan Professor of Chemistry Z n P A n Professor 4wliam H. me Johnson 3 Acknowledgments There are many people who helped make it possible for me to write this thesis. First and foremost, I must thank Steve Lippard for providing me the opportunity to join his research group at MIT. He allowed me to work independently, yet provided me much support and encouragement over the last five years. Studying the MMO system has led us down a variety of paths, and he was never hesitant to let me pursue new directions. I would also like to thank JoAnne Stubbe, William Orme-Johnson, and Alan Davison for serving on my thesis committee. I was fortunate to collaborate with may people away from MIT on several projects. Vickie DeRose and Brian Hoffman are responsible for many exciting EPR discoveries.
    [Show full text]
  • 255Th ACS National Spring Meeting Nitrogen Un
    255th ACS National Spring Meeting March 18-22, 2018 New Orleans, LA Nitrogen Un-Fixation: Mechanisms & Models of Nitrification/Denitrification Reactions Organizers Kyle Lancaster (Cornell University) Nicolai Lehnert (University of Michigan) Sunday, March 18 – SESSION 01 (MORNING) Ernest N. Morial Convention Center Room 210 Chair: Kyle Lancaster (Cornell) 8:30 Nitrite-ammonia expressway, with no stop at dinitrogen. Peter Kroneck 9:00 Evolution and modularity of ammonia oxidation pathways. Lisa Stein 9:30 Evaluating the Mechanism of NO Reduction in a Flavodiiron Nitric Oxide Reductase Model Complex. Corey White 9:50 Nitrous oxide reduction mediated by a nucleophilic nickel(II) sulfide. Trevor Hayton 10:20 Intermission. 10:30 Structure and function of particulate methane monooxygenase, an ammonia monooxygenase homolog. Amy Rosenzweig 11:00 Synthetic copper-sulfide models of CuZ with activity towards N2O and other small molecules. Neal Mankad 11:30 Revision by enzymology of bacterial ammonia oxidation. Jon Caranto 11:50 Probing Mechanisms of Nitrous Oxide Generation in a De- nitrifying Polyphosphate Accumulating Bacteria Enrichment Culture. George Wells Sunday, March 18 – SESSION 02 (AFTERNOON) Ernest N. Morial Convention Center Room 210 Chair: Sean Elliott (Boston University) 1:30 Bioinorganic aspects of nitrogen monoxide (NO) oxidation or reduction chemistry mediated at copper or heme centers. Ken Karlin 2:00 A Missing Link from Nitric Oxide to Nitrite in Ammonia Oxidizing Bacteria. Kyle Lancaster 2:30 Investigation of enzymatic N2O production through isotopic analysis and engineered enzymes. Clarisse Finders 2:50 Mechanistic studies of denitrifying heme-nonheme nitric oxide reductases.** Pierre Moenne-Loccoz 3:20 Intermission. 3:30 A metallopeptide functional mimic of cytochrome c nitrite reductase.
    [Show full text]
  • Faculty Recognition Dinner
    The 32nd Annual FACULTY RECOGNITION DINNER Kellogg Global Hub January 29, 2020 The 32nd Annual FACULTY RECOGNITION DINNER Hosted by President Morton Schapiro and Provost Jonathan Holloway, the annual Faculty Recognition Dinner honors Northwestern faculty who have brought distinction to the University by earning important external recognition in the past year. The Faculty Honors Committee reviewed award recipients identified by the deans and department chairs, selecting the most prestigious awards for University recognition. Each subcommittee reviewed awards in its respective fields. Arts and Humanities Life and Medical Chris Abani Sciences Richard Kieckhefer Serdar Bulun Sara Maza David Cella Saul Morson Bob Lamb Natasha Trethewey Sue Quaggin Amy Rosenzweig Engineering and Clyde Yancy Physical Sciences Wei Chen Social Sciences Yonggang Huang David Austen-Smith Bryna Kra Shari Diamond Tobin Marks Jamie Druckman Chad Mirkin Jan Eberly Greg Olson Larry Hedges Monica Olvera de la Cruz Joel Mokyr John Rogers Richard Silverman The Honorees Jan Achenbach Chaithanya Bandi Honorary Professor Faculty Award Xiamen University National Science Foundation Luis Amaral Zdeněk Bažant Fellow Foreign Associate American Institute for Medical Engineering Academy of Japan and Biological Engineering Foreign Member Sectional Committee for Engineering, Guillermo Ameer Royal Society Fellow National Academy of Inventors Karl Bilimoria Member Erik Andersen American Surgical Association Program Grants Award International Human Frontier Bruce Bochner Science Program
    [Show full text]