Serena DeBeer

Last updated
Prof. Dr.

Serena DeBeer
Born1973 (1973)
NationalityAmerican
Other namesSerena DeBeer George
EducationSouthwestern University, TX B.S. Chemistry (1995)
Stanford University Ph.D. Chemistry (2002)
Known for X-ray spectroscopy
nitrogenase
photosystem II
hydrogenase
Methane monooxygenase
Scientific career
Fields Chemistry
Institutions SSRL SLAC Stanford University (2001–2009)
Cornell University (2009-present)
Ruhr University Bochum (2014–present)
Max Planck Institute for Chemical Energy Conversion (2011–present)
Doctoral advisor Edward I. Solomon
Keith O. Hodgson

Serena DeBeer (born 1973) is an American chemist. She is currently a W3-Professor and the director at the Max Planck Institute for Chemical Energy Conversion in Muelheim an der Ruhr, Germany, where she heads the Department of Inorganic Spectroscopy. Her expertise lies in the application and development of X-ray based spectroscopic methods as probes of electronic structure in biological and chemical catalysis.

Contents

Education and career

Serena DeBeer studied at Southwestern University, Georgetown, Texas (US), where she completed her bachelor program in chemistry, with minor in mathematics in 1995 (with honors). She received her doctorate from Stanford University in 2002, working under the guidance of Edward I. Solomon and Keith O. Hodgson. She then moved to SLAC National Accelerator Laboratory, where she worked first as a beamline scientist (2001–2003) at the Stanford Synchrotron Radiation Laboratory, and later as staff scientist (2003–2009). In the Fall of 2009, she relocated to Cornell University in Ithaca, NY (USA), where she accepted a faculty position as assistant professor at the department of chemistry and chemical biology. [1] In the Summer of 2011, she moved to Germany and started to work as a W2-Professor and research group leader at the Max Planck Institute for Bioinorganic Chemistry (since 2012 Max Planck Institute for Chemical Energy Conversion, MPI CEC) in Mülheim an der Ruhr, Germany. Since 2012 she has held the position of an adjunct professor at Cornell University as well as an honorary faculty position at Ruhr University Bochum since 2014. [2] DeBeer headed the research group "X-ray Spectroscopy" at MPI CEC until 2017 when she was appointed director at this institute and promoted to a W3-Professor. Currently she leads the department of "Inorganic Spectroscopy" [3] at MPI CEC. Additionally, she is the group leader of the PINK beamline [4] project at the Energy and Materials In-Situ Laboratory [5] at the Helmholtz Zentrum Berlin, Germany.

Research

Research in the DeBeer group focuses on answering  fundamental questions in energy research. Namely, how does one reversibly store and release energy from chemical bonds using earth abundant transition metals? And how is this done most efficiently? Her research group studies homogeneous, heterogeneous and biological catalysts in order to answer these questions, with a primary focus on enzymatic catalysis. She is an expert in the application of advanced X-ray spectroscopy to understand catalytic transformations.

Nitrogenase

A strong focus of her research is to study the enzyme that is responsible for the conversion of dinitrogen (N2) to ammonia (NH3)—Nitrogenase. Serena DeBeer and her group study this remarkable system comprising a FeMo cofactor (FeMoco) as its active site, and structural model complexes utilizing high-resolution X-ray absorption (XAS) and X-ray emission spectroscopy (XES). Through this work, great progress has been made in understanding the structure of this active site. A key contribution was a spectroscopic identification of the central atom in the active site as a carbide. [6] Moreover, the application of high-resolution XAS spectroscopy supported with theoretical calculations, allowed her group to succeed in the assignment of the oxidation state of the Mo atom in the FeMoco as Mo(III). [7] This study was followed up later with the experimental evidence of a non-Hund spin configuration at the Mo atom by means of X-ray Magnetic Circular Dichroism (XMCD) spectroscopy. [8] Another approach in this field concerns comparative studies of different forms of nitrogenase enzymes with FeMoco and FeVco active sites, [9] Selenium-incorporated FeMoco, [10] as well as spectroscopic characterization of the first intermediate state of the nitrogenase catalytic cycle (E1). [11] [12]

Methane monooxygenase

Another important chemical conversion studied by her group is the catalytic oxidation of methane to methanol. Nature utilizes a group of enzymes called methane monooxygenase (MMOs). The active site of this enzyme that enables the cleavage of the C-H of methane is a dinuclear Fe(IV) intermediate Q found in the hydroxylase protein (MMOH) of MMO. Spectroscopic studies in the DeBeer group have provided new insights into the structure of this diiron complex. Through applications of advanced X-ray spectroscopic studies like high-resolution XAS they characterized the key intermediate in biological methane oxidation as an open-core diiron structure (with FeIV=O motif). [13] Additional EXAFS studies confirmed this finding by showing no evidence for a short Fe-Fe distance but rather a long diiron distance consistent with an open-core structure. [14]

Spectroscopy Development

Recent work of DeBeer's group has focused on developing the full information content of various X-ray spectroscopic methods and their application to biological catalysts.

Among these methods are:

Valence X-ray Emission Spectroscopy

In this method (also known as VtC XES = Valence-to-Core X-ray Emission Spectroscopy), one monitors the resultant fluorescence after a valence electron refills the ionized metal 1s core hole. As such, valence XES spectra provide a map of ligand ionization energies, and provides information on both ligand identity and protonation state. A prominent application of this method its use to identify the central carbon atom in FeMo cofactor of Nitrogenase (see section Nitrogenase). [6]

Resonant valence XES (RXES) or Resonant Inelastic X-ray Scattering (RIXS)

The DeBeer group is actively involved in the development and application of RXES/RIXS based methods in both the hard and soft X-ray regime. These include 1s-Valence RIXS as a means to obtain ligand-selective XAS [15] and 2p3d RIXS as a means to map out the d-d excitations. [16] [17] [18] [19] [20] [21]

X-ray Magnetic Circular Dichroism (XMCD)

This method has been extensively used in solid-state materials, to determine the magnetic properties. Past applications to (bio-)inorganic or protein systems were lacking proper qualitative and quantitative interpretations. DeBeer's group expanded the information that can be obtained from XMCD of covalent systems. [22] To date, this been the only one method able to provide evidence for the proposed non-Hund configuration at the Mo atom in Nitrogenase [8] (see section Nitrogeanse).

Instrumentation

A laboratory based dispersive X-ray Emission Spectrometer

The group of Serena DeBeer in collaboration with the group of Prof. Birgit Kangießer at TU Berlin, developed an in-house dispersive X-ray Emission Spectroscopy (XES) setup. The setup that utilizes a laboratory X‑ray source (Metal Jet) in combination with a von Hamos full cylinder optic with Highly Annealed Pyrolytic Graphite (HAPG) crystal and a CCD detector. This allows obtaining spectra in the 2.4-9 keV range. Moreover, this spectrometer is an alternative to synchrotron-based beamlines for concentrated samples. [23]

PINK Beamline

The DeBeer group is also leading the development of the PINK beamline [4] at the Energy Materials In-situ Laboratory [5] at the Helmholtz Zentrum Berlin. Dr. Sergey Peredkov is the lead designer and instrument scientist for this project. This beamline operates in 2-10 keV energy regime, either in a “pink” beam mode with multilayer mirror or with monochromatic beam (by addition of a double crystal monochromator). The beamline is presently in a commissioning phase.

Awards and recognition

Related Research Articles

<span class="mw-page-title-main">Nitrogenase</span> Class of enzymes

Nitrogenases are enzymes (EC 1.18.6.1EC 1.19.6.1) that are produced by certain bacteria, such as cyanobacteria (blue-green bacteria) and rhizobacteria. These enzymes are responsible for the reduction of nitrogen (N2) to ammonia (NH3). Nitrogenases are the only family of enzymes known to catalyze this reaction, which is a key step in the process of nitrogen fixation. Nitrogen fixation is required for all forms of life, with nitrogen being essential for the biosynthesis of molecules (nucleotides, amino acids) that create plants, animals and other organisms. They are encoded by the Nif genes or homologs. They are related to protochlorophyllide reductase.

The Max Planck Institute for Chemical Energy Conversion is a research institute of the Max Planck Society. It is located in the German town of Mülheim.

In chemistry, a (redox) non-innocent ligand is a ligand in a metal complex where the oxidation state is not clear. Typically, complexes containing non-innocent ligands are redox active at mild potentials. The concept assumes that redox reactions in metal complexes are either metal or ligand localized, which is a simplification, albeit a useful one.

Iron nitrides are inorganic chemical compounds of iron and nitrogen.

<span class="mw-page-title-main">FeMoco</span> Cofactor of nitrogenase

FeMoco (FeMo cofactor) is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric nitrogen molecules N2 into ammonia (NH3) through the process known as nitrogen fixation. Studying FeMoco's role in the reaction mechanism for nitrogen fixation is a potential use case for quantum computers. Even limited quantum computers could enable better simulations of the reaction mechanism.

<span class="mw-page-title-main">Abhik Ghosh</span> Indian chemist

Abhik Ghosh is an Indian inorganic chemist and materials scientist and a professor of chemistry at UiT – The Arctic University of Norway in Tromsø, Norway.

Lawrence Que Jr. is a chemist who specializes in bioinorganic chemistry and is a Regents Professor at the University of Minnesota, Twin Cities. He received the 2017 American Chemical Society (ACS) Award in Inorganic Chemistry for his contributions to the field., and the 2008 ACS Alfred Bader Award in Bioinorganic Chemistry.

Julia A. Kovacs is an American chemist specializing in bioinorganic chemistry. She is professor of chemistry at the University of Washington. Her research involves synthesizing small-molecule mimics of the active sites of metalloproteins, in order to investigate how cysteinates influence the function of non-heme iron enzymes, and the mechanism of the oxygen-evolving complex (OEC).

An oxyhydride is a mixed anion compound containing both oxide O2− and hydride ions H−. These compounds may be unexpected as the hydrogen and oxygen could be expected to react to form water. But if the metals making up the cations are electropositive enough, and the conditions are reducing enough, solid materials can be made that combine hydrogen and oxygen in the negative ion role.

The selenide iodides are chemical compounds that contain both selenide ions (Se2−) and iodide ions (I−) and one or metal atoms. They are in the class of mixed anion compounds or chalcogenide halides.

The iodate fluorides are chemical compounds which contain both iodate and fluoride anions (IO3− and F−). In these compounds fluorine is not bound to iodine as it is in fluoroiodates.

A selenite fluoride is a chemical compound or salt that contains fluoride and selenite anions. These are mixed anion compounds. Some have third anions, including nitrate, molybdate, oxalate, selenate, silicate and tellurate.

Borate sulfides are chemical mixed anion compounds that contain any kind of borate and sulfide ions. They are distinct from thioborates in which sulfur atoms replace oxygen in borates. There are also analogous borate selenides, with selenium ions instead of sulfur.

The borate bromides are mixed anion compounds that contain borate and bromide anions. They are in the borate halide family of compounds which also includes borate fluorides, borate chlorides, and borate iodides.

Karsten Meyer is a German inorganic chemist and Chair of Inorganic and General Chemistry at the Friedrich-Alexander University of Erlangen-Nürnberg (FAU). His research involves the coordination chemistry of transition metals as well as uranium coordination chemistry, small molecule activation with these coordination complexes, and the synthesis of new chelating ligands. He is the 2017 recipient of the Elhuyar-Goldschmidt Award of the Spanish Royal Society of Chemistry, the Ludwig-Mond Award of the Royal Society of Chemistry, and the L.A. Chugaev Commemorative Medal of the Russian Academy of Sciences, among other awards. He also serves as an Associate Editor of the journal Organometallics since 2014.

Connie C. Lu is a Taiwanese-American inorganic chemist and a professor of chemistry at the University of Minnesota, Twin Cities. Lu's research focuses on the synthesis of novel bimetallic coordination complexes, as well as metal-organic frameworks. These molecules and materials are investigated for the catalytic conversion of small molecules like as N2 and CO2 into value-added chemicals like ammonia and methanol. Lu is the recipient of multiple awards for her research, including the National Science Foundation CAREER Award and the Sloan Research Fellowship in 2013, and an Early Career Award from the University of Minnesota's Initiative for Renewable Energy and the Environment in 2010.

Selenogallates are chemical compounds which contain anionic units of selenium connected to gallium. They can be considered as gallates where selenium substitutes for oxygen. Similar compounds include the thiogallates and selenostannates. They are in the category of chalcogenotrielates or more broadly chalcogenometallates.

Sulfidostannates, or thiostannates are chemical compounds containing anions composed of tin linked with sulfur. They can be considered as stannates with sulfur substituting for oxygen. Related compounds include the thiosilicates, and thiogermanates, and by varying the chalcogen: selenostannates, and tellurostannates. Oxothiostannates have oxygen in addition to sulfur. Thiostannates can be classed as chalcogenidometalates, thiometallates, chalcogenidotetrelates, thiotetrelates, and chalcogenidostannates. Tin is almost always in the +4 oxidation state in thiostannates, although a couple of mixed sulfides in the +2 state are known,

Sulfidogermanates or thiogermanates are chemical compounds containing anions with sulfur atoms bound to germanium. They are in the class of chalcogenidotetrelates. Related compounds include thiosilicates, thiostannates, selenidogermanates, telluridogermanates and selenidostannates.

<span class="mw-page-title-main">Inverted ligand field theory</span>

Inverted ligand field theory (ILFT) describes a phenomenon in the bonding of coordination complexes where the lowest unoccupied molecular orbital is primarily of ligand character. This is contrary to the traditional ligand field theory or crystal field theory picture and arises from the breaking down of the assumption that in organometallic complexes, ligands are more electronegative and have fronteir orbitals below those of the d orbitals of electropositive metals. As we move to the right of the d-block and approach the transition-metal - main group boundary, the d orbitals become more core-like, making their cations more electronegative. This decreases their energies and eventually arrives at a point where they are lower in energy than the ligand fronteir orbitals. Here the ligand field inverts so that the bonding orbitals are more metal-based, and antibonding orbitals more ligand-based. The relative arrangement of the d orbitals are also inverted in complexes displaying this inverted ligand field. This has consequences in our understanding of accessible metal oxidation states, and the reactivity of complexes exhibiting ILFT.

References

  1. ↑ "Serena DeBeer | Chemistry & Chemical Biology Cornell Arts & Sciences".
  2. ↑ "Honorarprofessorin der RUB ist neue Direktorin". news.rub.de (in German). Retrieved 2019-08-08.
  3. ↑ "Prof. Dr. Serena DeBeer". cec.mpg.de. Retrieved 2019-12-02.
  4. 1 2 Energie, Helmholtz-Zentrum Berlin für Materialien und. "PINK". HZB Website. Retrieved 2019-12-02.
  5. 1 2 Energie, Helmholtz-Zentrum Berlin für Materialien und. "Energy Materials In-Situ Laboratory Berlin". HZB Website. Retrieved 2019-12-02.
  6. 1 2 Lancaster, K. M.; Roemelt, M.; Ettenhuber, P.; Hu, Y.; Ribbe, M. W.; Neese, F.; Bergmann, U.; DeBeer, S. (2011-11-18). "X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor". Science. 334 (6058): 974–977. Bibcode:2011Sci...334..974L. doi:10.1126/science.1206445. ISSN   0036-8075. PMC   3800678 . PMID   22096198.
  7. ↑ Bjornsson, Ragnar; Lima, Frederico A.; Spatzal, Thomas; Weyhermüller, Thomas; Glatzel, Pieter; Bill, Eckhard; Einsle, Oliver; Neese, Frank; DeBeer, Serena (2014). "Identification of a spin-coupled Mo(III) in the nitrogenase iron–molybdenum cofactor". Chem. Sci. 5 (8): 3096–3103. doi: 10.1039/C4SC00337C . ISSN   2041-6520.
  8. 1 2 Kowalska, Joanna K.; Henthorn, Justin T.; Van Stappen, Casey; Trncik, Christian; Einsle, Oliver; Keavney, David; DeBeer, Serena (2019-07-08). "X-ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin-Coupled Molybdenum(III) Center". Angewandte Chemie International Edition. 58 (28): 9373–9377. doi:10.1002/anie.201901899. PMC   6772009 . PMID   31119827.
  9. ↑ Rees, Julian A.; Bjornsson, Ragnar; Kowalska, Joanna K.; Lima, Frederico A.; Schlesier, Julia; Sippel, Daniel; Weyhermüller, Thomas; Einsle, Oliver; Kovacs, Julie A.; DeBeer, Serena (2017). "Comparative electronic structures of nitrogenase FeMoco and FeVco". Dalton Transactions. 46 (8): 2445–2455. doi:10.1039/C7DT00128B. ISSN   1477-9226. PMC   5322470 . PMID   28154874.
  10. ↑ Henthorn, Justin T.; Arias, Renee J.; Koroidov, Sergey; Kroll, Thomas; Sokaras, Dimosthenis; Bergmann, Uwe; Rees, Douglas C.; DeBeer, Serena (2019-08-28). "Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-Edge High Resolution X-ray Absorption Spectroscopy". Journal of the American Chemical Society. 141 (34): 13676–13688. doi:10.1021/jacs.9b06988. ISSN   0002-7863. PMC   6716209 . PMID   31356071.
  11. ↑ Van Stappen, Casey; Thorhallsson, Albert Thor; Decamps, Laure; Bjornsson, Ragnar; DeBeer, Serena (2019). "Resolving the structure of the E 1 state of Mo nitrogenase through Mo and Fe K-edge EXAFS and QM/MM calculations". Chemical Science. 10 (42): 9807–9821. doi: 10.1039/C9SC02187F . ISSN   2041-6520. PMC   6984330 . PMID   32055350.
  12. ↑ Van Stappen, Casey; Davydov, Roman; Yang, Zhi-Yong; Fan, Ruixi; Guo, Yisong; Bill, Eckhard; Seefeldt, Lance C.; Hoffman, Brian M.; DeBeer, Serena (2019-09-16). "Spectroscopic Description of the E 1 State of Mo Nitrogenase Based on Mo and Fe X-ray Absorption and Mössbauer Studies". Inorganic Chemistry. 58 (18): 12365–12376. doi:10.1021/acs.inorgchem.9b01951. ISSN   0020-1669. PMC   6751781 . PMID   31441651.
  13. ↑ Castillo, Rebeca G.; Banerjee, Rahul; Allpress, Caleb J.; Rohde, Gregory T.; Bill, Eckhard; Que, Lawrence; Lipscomb, John D.; DeBeer, Serena (2017-12-13). "High-Energy-Resolution Fluorescence-Detected X-ray Absorption of the Q Intermediate of Soluble Methane Monooxygenase". Journal of the American Chemical Society. 139 (49): 18024–18033. doi:10.1021/jacs.7b09560. ISSN   0002-7863. PMC   5729100 . PMID   29136468.
  14. ↑ Cutsail, George E.; Banerjee, Rahul; Zhou, Ang; Que, Lawrence; Lipscomb, John D.; DeBeer, Serena (2018-12-05). "High-Resolution Extended X-ray Absorption Fine Structure Analysis Provides Evidence for a Longer Fe···Fe Distance in the Q Intermediate of Methane Monooxygenase". Journal of the American Chemical Society. 140 (48): 16807–16820. doi:10.1021/jacs.8b10313. ISSN   0002-7863. PMC   6470014 . PMID   30398343.
  15. ↑ Hall, Eleanor R.; Pollock, Christopher J.; Bendix, Jesper; Collins, Terrence J.; Glatzel, Pieter; DeBeer, Serena (2014-07-16). "Valence-to-Core-Detected X-ray Absorption Spectroscopy: Targeting Ligand Selectivity". Journal of the American Chemical Society. 136 (28): 10076–10084. doi:10.1021/ja504206y. ISSN   0002-7863. PMID   24946007.
  16. ↑ Van Kuiken, Benjamin E.; Hahn, Anselm W.; Nayyar, Brahamjot; Schiewer, Christine E.; Lee, Sonny C.; Meyer, Franc; Weyhermüller, Thomas; Nicolaou, Alessandro; Cui, Yi-Tao; Miyawaki, Jun; Harada, Yoshihisa (2018-06-18). "Electronic Spectra of Iron–Sulfur Complexes Measured by 2p3d RIXS Spectroscopy". Inorganic Chemistry. 57 (12): 7355–7361. doi:10.1021/acs.inorgchem.8b01010. ISSN   0020-1669. PMID   29847108.
  17. ↑ Hahn, Anselm W.; Van Kuiken, Benjamin E.; al Samarai, Mustafa; Atanasov, Mihail; Weyhermüller, Thomas; Cui, Yi-Tao; Miyawaki, Jun; Harada, Yoshihisa; Nicolaou, Alessandro; DeBeer, Serena (2017-07-17). "Measurement of the Ligand Field Spectra of Ferrous and Ferric Iron Chlorides Using 2p3d RIXS". Inorganic Chemistry. 56 (14): 8203–8211. doi:10.1021/acs.inorgchem.7b00940. ISSN   0020-1669. PMID   28653856.
  18. ↑ Hahn, Anselm W.; Van Kuiken, Benjamin E.; Chilkuri, Vijay Gopal; Levin, Natalia; Bill, Eckhard; Weyhermüller, Thomas; Nicolaou, Alessandro; Miyawaki, Jun; Harada, Yoshihisa; DeBeer, Serena (2018-08-06). "Probing the Valence Electronic Structure of Low-Spin Ferrous and Ferric Complexes Using 2p3d Resonant Inelastic X-ray Scattering (RIXS)". Inorganic Chemistry. 57 (15): 9515–9530. doi:10.1021/acs.inorgchem.8b01550. ISSN   0020-1669. PMID   30044087. S2CID   51715606.
  19. ↑ Van Kuiken, Benjamin E.; Hahn, Anselm W.; Maganas, Dimitrios; DeBeer, Serena (2016-11-07). "Measuring Spin-Allowed and Spin-Forbidden d–d Excitations in Vanadium Complexes with 2p3d Resonant Inelastic X-ray Scattering". Inorganic Chemistry. 55 (21): 11497–11501. doi:10.1021/acs.inorgchem.6b02053. ISSN   0020-1669. PMID   27731986.
  20. ↑ Maganas, Dimitrios; DeBeer, Serena; Neese, Frank (2017-10-02). "A Restricted Open Configuration Interaction with Singles Method To Calculate Valence-to-Core Resonant X-ray Emission Spectra: A Case Study". Inorganic Chemistry. 56 (19): 11819–11836. doi:10.1021/acs.inorgchem.7b01810. ISSN   0020-1669. PMC   5692824 . PMID   28920680.
  21. ↑ Al Samarai, Mustafa; Hahn, Anselm W.; Beheshti Askari, Abbas; Cui, Yi-Tao; Yamazoe, Kosuke; Miyawaki, Jun; Harada, Yoshihisa; Rüdiger, Olaf; DeBeer, Serena (2019-10-23). "Elucidation of Structure–Activity Correlations in a Nickel Manganese Oxide Oxygen Evolution Reaction Catalyst by Operando Ni L-Edge X-ray Absorption Spectroscopy and 2p3d Resonant Inelastic X-ray Scattering". ACS Applied Materials & Interfaces. 11 (42): 38595–38605. doi: 10.1021/acsami.9b06752 . ISSN   1944-8244. PMID   31523947.
  22. ↑ Kowalska, Joanna K.; Nayyar, Brahamjot; Rees, Julian A.; Schiewer, Christine E.; Lee, Sonny C.; Kovacs, Julie A.; Meyer, Franc; Weyhermüller, Thomas; Otero, Edwige; DeBeer, Serena (2017-07-17). "Iron L 2,3 -Edge X-ray Absorption and X-ray Magnetic Circular Dichroism Studies of Molecular Iron Complexes with Relevance to the FeMoco and FeVco Active Sites of Nitrogenase". Inorganic Chemistry. 56 (14): 8147–8158. doi:10.1021/acs.inorgchem.7b00852. ISSN   0020-1669. PMC   5516708 . PMID   28653855.
  23. ↑ Malzer, Wolfgang; Grötzsch, Daniel; Gnewkow, Richard; Schlesiger, Christopher; Kowalewski, Fabian; Van Kuiken, Benjamin; DeBeer, Serena; Kanngießer, Birgit (November 2018). "A laboratory spectrometer for high throughput X-ray emission spectroscopy in catalysis research". Review of Scientific Instruments. 89 (11): 113111. Bibcode:2018RScI...89k3111M. doi: 10.1063/1.5035171 . ISSN   0034-6748. PMID   30501328.
  24. ↑ "ERC Synergy Grant for Serena DeBeer and an international and interdisciplinary team". cec.mpg.de. Retrieved 2019-11-27.
  25. ↑ "ERC 2019 Synergy Grants examples". ERC: European Research Council. 2019-10-10. Retrieved 2019-11-27.
  26. ↑ "Serena DeBeer joins Chemical Science as an Associate Editor – Chemical Science Blog" . Retrieved 2019-11-27.
  27. ↑ "Dr. Serena Debeer - 2016 Inorganic Chemistry Le... | ACS Network". communities.acs.org. Retrieved 2019-11-27.
  28. ↑ "Serena DeBeer SBIC Early Career Award".{{cite web}}: CS1 maint: url-status (link)
  29. ↑ "ERC Consolidator Grant: N2ase".{{cite web}}: CS1 maint: url-status (link)
  30. ↑ "Serena DeBeer". www.nasonline.org. Retrieved 2019-11-27.
  31. ↑ "Past Fellows". sloan.org. Archived from the original on 2018-03-14. Retrieved 2019-11-27.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.