2018 FACULTY RECOGNITION DINNER the Honorees
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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. -
Chad A. Mirkin, Ph.D
Chad A. Mirkin, Ph.D. Controlling the architecture of bio- or nonbio-materials in nanometer length scale and the application of such structures in the development of new technologies in diverse areas, such as chemical and biological sensing, gene regulation, lithography, catalysis, optics, and energy generation, storage, and conversion, are recognized to be one of the hottest research area. Chad Mirkin, who is a chemist, chemical engineer, and world-renowned expert in nanoscience, has contributed significantly in this field. He has pioneered the use of nanoparticle-biomolecule conjugates as synthons in materials science, their novel applications to extra- and intra-cellular diagnostic and therapeutic tools, and Dip-Pen Nanolithography. A common strategy used by Mirkin’s group is the use of the unique properties of spherical nucleic acids (SNAs), spherical arrangements of nucleic acids with or without organic or inorganic nanoparticle cores, to enable the synthesis of novel materials and development of highly sensitive probes for chemical and medical purposes. He is one of today’s most celebrated chemists for his discovery and development of SNAs and many medical diagnostic and therapeutic technologies, the invention of Dip-Pen Nanolithography (recognized by National Geographic as one of the top 100 scientific discoveries that changed the world), and significant contributions to supramolecular chemistry, nanoelectronics, and nanooptics. He is the author of over 700 manuscripts and over 1000 patents worldwide (over 300 issued), and the founder of six companies including Nanosphere, Nanolnk, AuraSense, Exicure, TERA-print, and CDJ, which are commercializing nanotechnology applications in the life science and semiconductor industries. He was an eight-year Member of the President’s Council of Advisors on Science & Technology (PCAST, Obama Administration), and the only chemist to be elected to all three US National Academies. -
Remarks by the Chair Chemistry Department
Chemistry Department Newsletter Summer 2004 Volume 2 http://www.dickinson.edu/departments/chem Remarks by the Chair Professor David Crouch Remarks by the Chair …..1 The Chemistry Department at Dickinson has enjoyed a most exciting year! New academic initiatives, major grants received, visiting faculty, Faculty Reports………2-4 renovations to Althouse and planning for the next phase of construction at Scholarly Research…….4-5 Dickinson have been part of the ways we have spent our time outside of the Department News……...5-7 classroom. The chemistry class of 2004 is moving on to some prestigious graduate and professional programs. One colleague was promoted to full 2004 Department Awards..7 professor and another has become a first time parent. A chemistry alum Class of 2004………..….…8 visited in the fall to tell us of his groundbreaking work in nanotechnology Recent Grad Spotlight…8-9 and returned in May to be honored by his alma mater with an honorary degree. This newsletter will fill in many of these details. But I’d like to Alumni News…………10-11 highlight three of them. Over the last few years, the possibility of developing an interdisciplinary major in neuroscience has been the subject of informal discussions around campus. In the fall, a committee was formed to formally prepare a proposed neuroscience major and, given chemistry’s role as the central science, it’s not surprising that two members of the chemistry department were involved. In the spring semester, the new major was officially adopted and the first neuroscience majors are being declared at Dickinson. The major consists of courses in psychology, biology and chemistry and new neuroscience courses at the 100 and 400 level are in development. -
Nanoparticle‐Mediated DNA and Mrna Delivery
REVIEW www.advhealthmat.de Next-Generation Vaccines: Nanoparticle-Mediated DNA and mRNA Delivery William Ho, Mingzhu Gao, Fengqiao Li, Zhongyu Li, Xue-Qing Zhang,* and Xiaoyang Xu* organism-based vaccines have wiped out or Nucleic acid vaccines are a method of immunization aiming to elicit immune nearly eradicated many once great killers responses akin to live attenuated vaccines. In this method, DNA or messenger of humanity, including smallpox, polio, RNA (mRNA) sequences are delivered to the body to generate proteins, which measles, mumps, rubella, diphtheria, per- [1–4] mimic disease antigens to stimulate the immune response. Advantages of tussis, and tetanus. However, the quick emergence of diseases such as SARS- nucleic acid vaccines include stimulation of both cell-mediated and humoral CoV-2, H1N1 as well as quickly evolving immunity, ease of design, rapid adaptability to changing pathogen strains, and deadly diseases like Ebola create a challenge customizable multiantigen vaccines. To combat the SARS-CoV-2 pandemic, for conventional vaccines such as live at- and many other diseases, nucleic acid vaccines appear to be a promising tenuated viral vaccines (LAV), and inacti- [5,6] method. However, aid is needed in delivering the fragile DNA/mRNA payload. vated/killed viral vaccines, which with Many delivery strategies have been developed to elicit effective immune the traditional vaccine development path- way may take on average over 10 years to stimulation, yet no nucleic acid vaccine has been FDA-approved for human develop, or with Ebola requiring an acceler- use. Nanoparticles (NPs) are one of the top candidates to mediate successful ated 5-year development,[7] and even more DNA/mRNA vaccine delivery due to their unique properties, including time needed to scale up manufacturing and unlimited possibilities for formulations, protective capacity, simultaneous stockpile for a large country. -
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. -
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. -
AAAFM-UCLA, 2019 August Aug 19-22, 2019, UCLA Prof. Chad Mirkin
AAAFM-UCLA, 2019 August Aug 19-22, 2019, UCLA Prof. Chad Mirkin H-Index (Google Scholar): 163 Director, International Institute for Nanotechnology, Northwestern University Dr. Chad A. Mirkin is the Director of the International Institute for Nanotechnology, the George B. Rathmann Professor of Chemistry, Professor of Chemical and Biological Engineering, Professor of Biomedical Engineering, Professor of Materials Science and Engineering, and Professor of Medicine. Professor Mirkin is a chemist and a world renowned nanoscience expert, who is known for his development of nanoparticle-based biodetection schemes, the invention of Dip-Pen Nanolithography, and contributions to supramolecular chemistry, nanoelectronics and nanooptics. He is the author of over 380 manuscripts and over 350 patents and applications, and the founder of two companies, Nanosphere and NanoInk, which are commercializing nanotechnology applications in the life science and semiconductor industries. Currently, he is listed as the third most cited chemist in the world, and is the top most cited nanomedicine researcher in the world. At present, he is a member of the President Obama’s Council of Advisors for Science and Technology. Dr. Mirkin has been recognized for his accomplishments with over 50 national and international awards. These include the Lemelson-MIT Prize, Havinga Medal, the Gustavus John Esselen Award, the Biomedical Engineering Society’s Distinguished Achievement Award, a Department of Defense NSSEFF Award, the Pittsburgh Analytical Chemistry Award, the ACS -
“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 -
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. -
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. -
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. -
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.