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Julie Kovacs

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Julia A. Kovacs
Born
Julia Ann Kovacs

(1959-03-15) March 15, 1959 (age 65)[1]
Alma materMichigan State University BS (1981)
Harvard University Ph.D. (1986)
Scientific career
FieldsBioinorganic chemistry
InstitutionsUniversity of Washington
ThesisVanadium-Iron-Sulfur and Molybdenum-Iron-Sulfur Cluster Chemistry (Nitrogenase) (1986)
Doctoral advisorRichard H. Holm
Other academic advisorsBruce Averill, Robert G. Bergman
Notable studentsJason M. Shearer
Websitedepts.washington.edu/kovaclab/kovacslab/index.html

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).

Early life and education

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Kovacs completed her undergraduate degree at Michigan State University, graduating with a B.S. in chemistry in 1981.[2] There, she worked with Prof. Bruce Averill on the synthesis of iron-sulfur cluster compounds, which mimic the FeMo-cofactor of nitrogenase.[3] She then moved to Harvard University for graduate studies, and there she continued her work on iron-sulfur clusters with Prof. Richard H. Holm.[4][5][6][7][8] Kovacs graduated with her PhD in 1986.[9] She then moved to California to conduct postdoctoral research at the University of California, Berkeley, where she worked with Prof. Robert G. Bergman on heterobimetallic sulfur-bridged complexes.[10][11]

Research and career

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Kovacs began her independent research career in 1988 when she joined the University of Washington as an assistant professor. She was promoted to associate professor in 1994, then further promoted to full professor in 2001. She was chair of the American Chemical Society Division of Inorganic Chemistry in 2020.[12]

Kovacs' research involves investigations into the role of thiolates in dioxygen chemistry.[13] Non-heme iron enzymes are known to promote biological reactions, but the mechanisms by which cysteinates impact their function are not well understood.[14]

Kovacs is interested in the formation of the oxygen–oxygen bond.[15][16] In nature, it is this oxygen-evolving complex (OEC) that stores solar energy in chemical bonds. By creating a series of small molecule analogues, Kovacs studies the radical coupling mechanism by which MnIV-oxyl radicals attach bridging oxo groups. She also investigates nucleophilic attack of MnV-oxo due to hydroxyl groups on the OEC. The small molecules include nitrogen and sulphur and a particular stereochemistry. Through synthesis of organic molecules with a variety of different molecular frameworks, Kovacs investigates their structure-property relationships and the reactivity of the resulting transition-metal complexes.[17][18] Kovacs has also studied the activity of meta-stable thiolate-ligated manganese peroxo intermediates.[19][20][21]

Selected publications

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Her publications include:

  • Synthetic analogues of cysteinate-ligated non-heme iron and non-corrinoid cobalt enzymes (DOI: 10.1021/cr020619e)[22]
  • Synthetic Models for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase:  Observation and Structural Characterization by XAS of an FeIII−OOH Intermediate (DOI: 10.1021/ja012722b)[23]
  • Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase (DOI: 10.1021/ar600059h)[24]

Personal life

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References

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  1. ^ Kovacs, Julie A.; Brines, Lisa M. (2007-10-02). "Understanding How the Thiolate Sulfur Contributes to the Function of the Non-Heme Iron Enzyme Superoxide Reductase". ChemInform. 38 (40): 501–509. doi:10.1002/chin.200740273. ISSN 0931-7597. PMC 3703784. PMID 17536780.
  2. ^ harva015 (2019-09-12). "Department Seminar: Professor Julie A. Kovacs". Department of Chemistry. Retrieved 2020-03-09.{{cite web}}: CS1 maint: numeric names: authors list (link)
  3. ^ Bose, K.S.; Lamberty, P.E.; Kovacs, J.E.; Sinn, E.; Averill, B.A. (1986-01-01). "Synthesis of a new class of Mo-Fe-S clusters containing the MoS2Fe2 unit". Polyhedron. 5 (1–2): 393–398. doi:10.1016/S0277-5387(00)84939-6. ISSN 0277-5387.
  4. ^ Kovacs, Julie A.; Bashkin, J. K.; Holm, R. H. (March 1985). "Persulfide-bridged iron-molybdenum-sulfur clusters of biological relevance: two synthetic routes and the structures of intermediate and product clusters". Journal of the American Chemical Society. 107 (6): 1784–1786. doi:10.1021/ja00292a067. ISSN 0002-7863.
  5. ^ Kovacs, Julie A.; Holm, R. H. (1986-01-01). "Assembly of vanadium-iron-sulfur cubane clusters from mononuclear and linear trinuclear reactants". Journal of the American Chemical Society. 108 (2): 340–341. doi:10.1021/ja00262a050. ISSN 0002-7863.
  6. ^ Kovacs, Julie A.; Holm, Richard H. (March 1987). "Heterometallic clusters: synthesis and reactions of vanadium-iron-sulfur single- and double-cubane clusters and the structure of [V2Fe6S8Cl4(C2H4S2)2]4-". Inorganic Chemistry. 26 (5): 702–711. doi:10.1021/ic00252a014. ISSN 0020-1669.
  7. ^ Kovacs, Julie A.; Holm, Richard H. (March 1987). "Structural chemistry of vanadium-iron-sulfur clusters containing the cubane-type [VFe3S4]2+ core". Inorganic Chemistry. 26 (5): 711–718. doi:10.1021/ic00252a015. ISSN 0020-1669.
  8. ^ Kovacs, Julie A.; Bashkin, James K.; Holm, R.H. (1987-01-01). "[Fe2S2(CO)6]2− as a cluster precursor: synthesis and structure of [MoFe3S6(CO)6]2− and oxidative decarbonylation to a persulfide-bridged MoFe3S4 double cubane". Polyhedron. 6 (6): 1445–1456. doi:10.1016/S0277-5387(00)80908-0. ISSN 0277-5387.
  9. ^ "Kovacs Lab Members". depts.washington.edu. Retrieved 2020-03-09.
  10. ^ "Former Bergman Group Members – Bergman Group". Retrieved 2020-03-09.
  11. ^ Kovacs, Julie A.; Bergman, Robert G. (February 1989). "Synthesis and reactivity of the first structurally characterized heterobimetallic complex containing an unsupported bridging sulfur atom". Journal of the American Chemical Society. 111 (3): 1131–1133. doi:10.1021/ja00185a055. ISSN 0002-7863.
  12. ^ "Julie Kovacs elected Chair of the ACS Division of Inorganic Chemistry | Department of Chemistry | University of Washington". chem.washington.edu. Retrieved 2021-05-17.
  13. ^ Kovacs, Julie A. (2003-02-14). "How Iron Activates O2". Science. 299 (5609): 1024–1025. doi:10.1126/science.1081792. ISSN 0036-8075. PMID 12586930. S2CID 93705834.
  14. ^ Shearer, Jason; Scarrow, Robert C.; Kovacs, Julie A. (2002-10-01). "Synthetic Models for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase: Observation and Structural Characterization by XAS of an FeIII−OOH Intermediate". Journal of the American Chemical Society. 124 (39): 11709–11717. doi:10.1021/ja012722b. ISSN 0002-7863. PMID 12296737.
  15. ^ "Kovacs Lab Research". depts.washington.edu. Retrieved 2020-03-09.
  16. ^ "NSF Award Search: Award#1664682 - Understanding the Mechanism of Mn-Promoted H2O Oxidation". www.nsf.gov. Retrieved 2020-03-09.
  17. ^ "Julie A. Kovacs - UW Dept. of Chemistry". depts.washington.edu. Retrieved 2020-03-09.
  18. ^ Yan Poon, Penny Chaau; Dedushko, Maksym A.; Sun, Xianru; Yang, Guang; Toledo, Santiago; Hayes, Ellen C.; Johansen, Audra; Piquette, Marc C.; Rees, Julian A.; Stoll, Stefan; Rybak-Akimova, Elena (2019-09-25). "How Metal Ion Lewis Acidity and Steric Properties Influence the Barrier to Dioxygen Binding, Peroxo O–O Bond Cleavage, and Reactivity". Journal of the American Chemical Society. 141 (38): 15046–15057. doi:10.1021/jacs.9b04729. ISSN 0002-7863. PMID 31480847. S2CID 201831519.
  19. ^ Coggins, Michael K.; Martin-Diaconescu, Vlad; DeBeer, Serena; Kovacs, Julie A. (2013-03-20). "Correlation Between Structural, Spectroscopic, and Reactivity Properties Within a Series of Structurally Analogous Metastable Manganese(III)–Alkylperoxo Complexes". Journal of the American Chemical Society. 135 (11): 4260–4272. doi:10.1021/ja308915x. ISSN 0002-7863. PMC 3740743. PMID 23432090.
  20. ^ Coggins, Michael K.; Sun, Xianru; Kwak, Yeonju; Solomon, Edward I.; Rybak-Akimova, Elena; Kovacs, Julie A. (2013-04-17). "Characterization of Metastable Intermediates Formed in the Reaction between a Mn(II) Complex and Dioxygen, Including a Crystallographic Structure of a Binuclear Mn(III)–Peroxo Species". Journal of the American Chemical Society. 135 (15): 5631–5640. doi:10.1021/ja311166u. ISSN 0002-7863. PMC 3709604. PMID 23470101.
  21. ^ Rees, Julian A.; Martin-Diaconescu, Vlad; Kovacs, Julie A.; DeBeer, Serena (2015-06-10). "X-ray Absorption and Emission Study of Dioxygen Activation by a Small-Molecule Manganese Complex". Inorganic Chemistry. 54 (13): 6410–6422. doi:10.1021/acs.inorgchem.5b00699. ISSN 0020-1669. PMC 4494871. PMID 26061165.
  22. ^ Kovacs, Julie A. (2004-05-25). "Synthetic Analogues of Cysteinate-Ligated Non-Heme Iron and Non-Corrinoid Cobalt Enzymes". ChemInform. 35 (21): 825–848. doi:10.1002/chin.200421278. ISSN 0931-7597. PMC 4487544. PMID 14871143.
  23. ^ Shearer, Jason; Scarrow, Robert C.; Kovacs, Julie A. (2002). "Synthetic Models for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase: Observation and Structural Characterization by XAS of an Fe III −OOH Intermediate". Journal of the American Chemical Society. 124 (39): 11709–11717. doi:10.1021/ja012722b. ISSN 0002-7863. PMID 12296737.
  24. ^ Kovacs, Julie A.; Brines, Lisa M. (2007-10-02). "Understanding How the Thiolate Sulfur Contributes to the Function of the Non-Heme Iron Enzyme Superoxide Reductase". ChemInform. 38 (40): 501–509. doi:10.1002/chin.200740273. ISSN 0931-7597. PMC 3703784. PMID 17536780.
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