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Metallocofactors
Gordon Research Conference

Inorganic Components of Nature that Drive Metabolism

Dates

June 12-17, 2016

Location

Stonehill College
Easton, MA

Organizers

Chair:
Jonas C. Peters

Vice Chair:
Sean J. Elliott

Meeting Description

Metallocofactors are essential for all forms of life and can include iron, magnesium, manganese, cobalt, copper, zinc, nickel, and molybdenum. Much progress has been made towards understanding their roles in metabolism and exploring how such understanding might be advanced in support of human health and sustainability. Among the diverse range of metallocofactors found in biology are iron-sulfur (FeS) clusters that serve as prosthetic groups and facilitate unique chemistry in proteins, and FeS proteins that are represented in the most central metabolic pathways such as the citric acid cycle and the mitochondrial respiratory chain. FeS enzymes also play critical roles in the generation of radicals, as demonstrated by the very diverse family of SAM-dependent enzymes. Structurally fascinating metallocofactors featuring Fe, Mn, Mo, Ni, and Cu are present in many bacteria and mediate remarkable metabolic redox chemistry with small molecule substrates including N2, H2O, H2, CO2, N2O, and CH4. Current interest in understanding how these metallocofactors function at the atomic level is enormous, especially in the context of sustainably feeding and fueling our planet; if we can understand how these cofactors work, there exists the possibility to design synthetic catalysts that function similarly.

The 2016 Gordon Research Conference on Metallocofactors will highlight the recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors. This is a unique opportunity to bring young and distinguished researchers of various disciplines and backgrounds together in a manner that will be conducive to creative thinking and that has the potential to catalyze significant progress in metallocofactor research and understanding.

Contributors

Final Meeting Program

Sunday
2:00 pm - 9:00 pmArrival and Check-in
6:00 pmDinner
7:30 pm - 7:40 pmWelcome / Introductory Comments by GRC Site Staff
7:40 pm - 9:30 pmKeynote Session: Metallocofactors that Feed and Fuel Our Planet
Discussion Leader: Harry Gray (California Institute of Technology, USA)
7:40 pm - 8:20 pmJian-Ren Shen (Okayama University, Japan)
"How Does Photosystem II Split Water? A Structural Point of View"
8:20 pm - 8:35 pmDiscussion
8:35 pm - 9:15 pmBrian Hoffman (Northwestern University, USA)
"How Nitrogenase Activates N2"
9:15 pm - 9:30 pmDiscussion
Monday
7:30 am - 8:30 amBreakfast
9:00 am - 12:30 pmPhotosynthetic Cofactors in Biology
Discussion Leader: R. David Britt (University of California, Davis, USA)
9:00 am - 9:30 amJunko Yano (Lawrence Berkeley National Laboratory, USA)
"Taking Snapshots of Photosynthetic Water Oxidation"
9:30 am - 9:45 amDiscussion
9:45 am - 10:15 amWolfgang Lubitz (Max Planck Institute for Chemical Energy Conversion, Germany)
"Water Binding to the Oxygen Evolving Complex in Photosystem II"
10:15 am - 10:30 amDiscussion
10:30 am - 11:00 amCoffee Break
11:00 am - 11:30 amErwin Reisner (University of Cambridge, United Kingdom)
"Making Photosynthetic Cofactors Work in Semi-Artificial Solar Fuel Synthesis"
11:30 am - 11:45 amDiscussion
11:45 am - 12:15 pmDaniel Nocera (Harvard University, USA)
"An Artificial Oxygen Evolving Complex: From Self-Repair to the Kok Cycle"
12:15 pm - 12:30 pmDiscussion
12:30 pmLunch
1:30 pm - 4:00 pmFree Time
4:00 pm - 6:00 pmPoster Session
6:00 pmDinner
7:30 pm - 9:30 pmModeling the Structure and Function of Photosynthetic Cofactors
Discussion Leader: Theodore Betley (Harvard University, USA)
7:30 pm - 8:00 pmTheodor Agapie (California Institute of Technology, USA)
"Rational Synthesis of Complex Biological Active Site Models: Insights Regarding Function"
8:00 pm - 8:10 pmDiscussion
8:10 pm - 8:40 pmChunxi Zhang (Chinese Academy of Sciences, China)
"Artificial Mn4Ca-Cluster Mimicking the Oxygen-Evolving Center in Photosystem II"
8:40 pm - 8:50 pmDiscussion
8:50 pm - 9:20 pmPer E. Siegbahn (Stockholm University, Sweden)
"The O-O Bond Formation Mechanism in Photosystem II and in Biomimetics"
9:20 pm - 9:30 pmDiscussion
Tuesday
7:30 am - 8:30 amBreakfast
8:30 amGroup Photo
9:00 am - 12:30 pmNitrogenase Enzymes
Discussion Leader: Douglas Rees (California Institute of Technology / Howard Hughes Medical Institute, USA)
9:00 am - 9:30 amThomas Spatzal (California Institute of Technology, USA)
"Structural Dynamic of the Nitrogenase FeMo-Cofactor During Catalysis"
9:30 am - 9:45 amDiscussion
9:45 am - 10:15 amSerena Debeer (Max Planck Institute for Chemical Energy Conversion, Germany)
"Recent Insights into the Active Sites of Molybdenum and Vanadium Nitrogenases from Advanced X-Ray Spectroscopy"
10:15 am - 10:30 amDiscussion
10:30 am - 11:00 amCoffee Break
11:00 am - 11:30 amStephen Cramer (University of California, Davis, USA)
"N2ase-Substrate Binding: Synchrotron NRVS and Good Old FT-IR"
11:30 am - 11:45 amDiscussion
11:45 am - 12:00 pmSelected from Poster Abstracts: Lance Seefeldt (Utah State University, USA)
"Electro- and Photo-Catalytic Nitrogenase Reactions"
12:00 pm - 12:05 pmDiscussion
12:05 pm - 12:20 pmSelected from Poster Abstracts: Kyle Lancaster (Cornell University, USA)
"Forays in Nitrification Enzymology"
12:20 pm - 12:25 pmDiscussion
12:25 pm - 12:30 pmGeneral Discussion
12:30 pmLunch
1:30 pm - 4:00 pmFree Time
4:00 pm - 6:00 pmPoster Session
6:00 pmDinner
7:30 pm - 9:30 pmModeling the Structure and Function of Nitrogenase Cofactors
Discussion Leader: Connie Lu (University of Minnesota, USA)
7:30 pm - 8:00 pmFrank Neese (Max Planck Institute for Chemical Energy Conversion, Germany)
"Structure and Spectroscopy of Reactive Intermediates in Metalloenzymes and Model Systems"
8:00 pm - 8:10 pmDiscussion
8:10 pm - 8:40 pmLeslie Murray (University of Florida, USA)
"Binding and Activation of Small Molecules by Triiron Complexes"
8:40 pm - 8:50 pmDiscussion
8:50 pm - 9:20 pmPatrick Holland (Yale University, USA)
"The Quest for Iron-Based FeMoco Model Complexes with Sulfur-Based Ligands"
9:20 pm - 9:30 pmDiscussion
Wednesday
7:30 am - 8:30 amBreakfast
9:00 am - 12:30 pmAssembly, Structure, and Function of FeS-Cofactors
Discussion Leader: Joan Broderick (Montana State University, USA)
9:00 am - 9:30 amDeborah Perlstein (Boston University, USA)
"Cytosolic FeS Biosynthesis: Ironing out the Mechanistic Details"
9:30 am - 9:45 amDiscussion
9:45 am - 10:15 amSheila David (University of California, Davis, USA)
"The DNA Repair Glycosyase MUTYH: Mutations, Metal Cofactors and Medicine"
10:15 am - 10:30 amDiscussion
10:30 am - 11:00 amCoffee Break
11:00 am - 11:30 amAmie Boal (Pennsylvania State University, USA)
"Crystallographic Capture of a Radical SAM Enzyme in the Act of Modifying Transfer RNA"
11:30 am - 11:45 amDiscussion
11:45 am - 12:00 pmSelected from Poster Abstracts: Trevor Del Castillo (California Institute of Technology, USA)
"Studies on the Catalytic Fixation of N2 by Synthetic Fe Complexes"
12:00 pm - 12:05 pmDiscussion
12:05 pm - 12:20 pmSelected from Poster Abstracts: Anna Vagstad (ETH Zurich, Switzerland)
"Mechanistic Insights into Radical-Mediated Amino Acid Epimerization in Proteusin Peptide Natural Products"
12:20 pm - 12:25 pmDiscussion
12:25 pm - 12:30 pmGeneral Discussion
12:30 pmLunch
1:30 pm - 4:00 pmFree Time
4:00 pm - 6:00 pmPoster Session
6:00 pmDinner
7:00 pm - 7:30 pmBusiness Meeting
Nominations for the Next Vice Chair; Fill in Conference Evaluation Forms; Discuss Future Site and Scheduling Preferences; Election of the Next Vice Chair
7:30 pm - 9:30 pmFe and Ni Cofactors that Interact with O2, H2, and CO2
Discussion Leader: Fraser Armstrong (University of Oxford, United Kingdom)
7:30 pm - 8:00 pmRobert Hausinger (Michigan State University, USA)
"A New Ni-Containing Niacin-Derived Microbial Cofactor"
8:00 pm - 8:10 pmDiscussion
8:10 pm - 8:40 pmJuan Fontecilla-Camps (Institut de Biologie Structurale, France)
"Structure-Function Relationships of the Global Transcriptional Regulator FNR"
8:40 pm - 8:50 pmDiscussion
8:50 pm - 9:20 pmMichael Green (University of California, Irvine, USA)
"Exploring the Factors that Govern Biological C-H Bond Activation"
9:20 pm - 9:30 pmDiscussion
Thursday
7:30 am - 8:30 amBreakfast
9:00 am - 12:30 pmDe Novo Cofactor Design and Characterization
Discussion Leader: Yi Lu (University of Illinois, USA)
9:00 am - 9:30 amAkif Tezcan (University of California, San Diego, USA)
"Design and Evolution of Supramolecular Metalloenzymes"
9:30 am - 9:45 amDiscussion
9:45 am - 10:15 amThomas Ward (University of Basel, Switzerland)
"Artificial Metalloenzymes Bearing Precious Metal Cofactors"
10:15 am - 10:30 amDiscussion
10:30 am - 11:00 amCoffee Break
11:00 am - 11:30 amGiovanna Ghirlanda (Arizona State University, USA)
"Metalloenzymes by Design: Controlling the Reactivity of Artificial Cofactors"
11:30 am - 11:45 amDiscussion
11:45 am - 12:00 pmSelected from Poster Abstracts: Jennifer Bridwell-Rabb (Massachusetts Institute of Technology, USA)
"An Evolving Active Site in the HD-Domain Phosphorylhydrolase Responsible for Oxetanocin Biosynthesis"
12:00 pm - 12:05 pmDiscussion
12:05 pm - 12:20 pmSelected from Poster Abstracts: Manas Kumar Ghosh (Pennsylvania State University, USA)
"Structure and Mechanism of Assembly of a Novel Radical-Initiating Dimanganese Cofactor in Ribonucleotide Reductase from Flavobacterium johnsoniae"
12:20 pm - 12:25 pmDiscussion
12:25 pm - 12:30 pmGeneral Discussion
12:30 pmLunch
1:30 pm - 4:00 pmFree Time
4:00 pm - 6:00 pmPoster Session
6:00 pmDinner
7:30 pm - 9:30 pmKeynote Session: The Latest on Radical SAM Enzymes
Discussion Leader: Squire Booker (Pennsylvania State University, USA)
7:30 pm - 7:40 pmIntroduction by Discussion Leader
7:40 pm - 8:20 pmCatherine Drennan (Massachusetts Institute of Technology, USA)
"The Anatomy of a Radical Enzyme"
8:20 pm - 8:35 pmDiscussion
8:35 pm - 9:15 pmMarkus Ribbe (University of California, Irvine, USA)
"Radical SAM-Dependent Maturation of Nitrogenase Cofactor"
9:15 pm - 9:30 pmDiscussion
Friday
7:30 am - 8:30 amBreakfast
9:00 amDeparture

This material is based upon work supported by the U.S. Department of Energy, Office of Science, Office of Acquisition and Assistance, under Award Number DC-SC0015689. This report was prepared as an account of work sponsored by an agency of the United States Government. Neither the United States Government nor any agency thereof, nor any of their employees, makes any warranty, express or implied, or assumes any legal liability or responsibility for the accuracy, completeness, or usefulness of any information, apparatus, product, or process disclosed, or represents that its use would not infringe privately owned rights. Reference herein to any specific commercial product, process, or service by trade name, trademark, manufacturer, or otherwise does not necessarily constitute or imply its endorsement, recommendation, or favoring by the United States Government or any agency thereof. The views and opinions of authors expressed herein do not necessarily state or reflect those of the United States Government or any agency thereof.

Research reported in this publication was supported by the National Institute of General Medical Sciences of the National Institutes of Health under Award Number 1R13GM119223-01. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
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