Edward I. Solomon

Last updated
Edward I. Solomon
Born
Edward Ira Solomon

1946 (age 7677)
Nationality American
Alma mater Rensselaer Polytechnic Institute B.S. (1968)
Princeton University Ph.D. (1972)
Spouse Darlene Solomon
Scientific career
Fields Bioinorganic Chemistry, Spectroscopy, Theoretical Chemistry
Institutions Stanford University
Thesis The Jahn-Teller Effect in the Orbital Triplet Excited States of Octahedral Manganese(II)  (1972)
Doctoral advisor Donald S. McClure
Other academic advisorsCarl J. Ballhausen, Harry B. Gray
Doctoral students Serena DeBeer, Darlene Joy Spira
Other notable students Frank Neese
Website web.stanford.edu/group/solomon/home.html

Edward I. Solomon (born 1946) is the Monroe E. Spaght Professor of Chemistry at Stanford University. He is an elected member of the United States National Academy of Sciences, [1] a Fellow of the American Association for the Advancement of Science, and a Fellow of the American Academy of Arts and Sciences. [2] [3] He has been profiled in the Proceedings of the National Academy of Sciences. [4] He has also been a longtime collaborator with many scientists, including Professor Kenneth D. Karlin at Johns Hopkins University.

Contents

Early life and education

Solomon grew up in North Miami Beach, Florida. In his junior year of high school, he became involved in a local program that allowed exceptional students to work with university professors. Solomon conducted research with a professor at the University of Miami, using biochemistry and chromatography to study indoles, which led to him becoming Florida's first-ever finalist for the Westinghouse Science Talent Search in 1964. [5]

He then studied chemistry at Renesselaer Polytechnic Institute, graduating with a B.S. degree in 1968. During his undergraduate, he worked with Prof. Sam Wait and Prof. Henry Hollinger in theoretical chemistry. [5] Solomon went on to Princeton University to conduct graduate studies with physical chemist Prof. Donald McClure, where he studied the Jahn-Teller effect in the excited states of Mn2+ ions in RbMnF3. [6] [7] Shortly after Solomon received his Ph.D. in chemistry in 1972, his advisor McClure went on sabbatical and asked Solomon to stay and help oversee his research group. At this time, McClure and Prof. Thomas G. Spiro hosted a symposium that hosted many leaders in physical inorganic chemistry. It was at this symposium that Solomon decided he wanted to work with Prof. Harry B. Gray during his post-doctoral studies.

Solomon spent a year in Copenhagen, Denmark at the Hans Christian Ørsted Institute to work as a postdoctoral fellow under Prof. Carl J. Ballhausen. [8] He then moved to Caltech with to do postdoctoral research with Prof. Harry B. Gray from 1974 to 1975. [2]

Research

Solomon began his independent career in late 1975 at the Massachusetts Institute of Technology as an assistant professor, where he continued to study blue copper proteins. [5] In 1981, he was promoted to the rank of full professor, and in 1982 he moved to Stanford University. [2] At this point, bioinorganic chemistry became the dominant focus of his laboratory.

Solomon's research focuses on characterization of metal-containing enzymes. These include copper-containing enzymes such as azurin, plastocyanin and laccase, [9] as well as non-heme iron enzymes such as (4-hydroxy)mandelate synthase and (4-hydroxyphenyl)pyruvate dioxygenase. He is an expert in magnetic circular dichroism spectroscopy. [4]

Research highlights

Awards

Professional memberships

Related Research Articles

<span class="mw-page-title-main">Inorganic chemistry</span> Field of chemistry

Inorganic chemistry deals with synthesis and behavior of inorganic and organometallic compounds. This field covers chemical compounds that are not carbon-based, which are the subjects of organic chemistry. The distinction between the two disciplines is far from absolute, as there is much overlap in the subdiscipline of organometallic chemistry. It has applications in every aspect of the chemical industry, including catalysis, materials science, pigments, surfactants, coatings, medications, fuels, and agriculture.

Circular dichroism (CD) is dichroism involving circularly polarized light, i.e., the differential absorption of left- and right-handed light. Left-hand circular (LHC) and right-hand circular (RHC) polarized light represent two possible spin angular momentum states for a photon, and so circular dichroism is also referred to as dichroism for spin angular momentum. This phenomenon was discovered by Jean-Baptiste Biot, Augustin Fresnel, and Aimé Cotton in the first half of the 19th century. Circular dichroism and circular birefringence are manifestations of optical activity. It is exhibited in the absorption bands of optically active chiral molecules. CD spectroscopy has a wide range of applications in many different fields. Most notably, UV CD is used to investigate the secondary structure of proteins. UV/Vis CD is used to investigate charge-transfer transitions. Near-infrared CD is used to investigate geometric and electronic structure by probing metal d→d transitions. Vibrational circular dichroism, which uses light from the infrared energy region, is used for structural studies of small organic molecules, and most recently proteins and DNA.

<span class="mw-page-title-main">Plastocyanin</span>

Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it participates in photosynthesis. The protein is a prototype of the blue copper proteins, a family of intensely blue-colored metalloproteins. Specifically, it falls into the group of small type I blue copper proteins called "cupredoxins".

Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.

Laccases are multicopper oxidases found in plants, fungi, and bacteria. Laccases oxidize a variety of phenolic substrates, performing one-electron oxidations, leading to crosslinking. For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols. Other laccases, such as those produced by the fungus Pleurotus ostreatus, play a role in the degradation of lignin, and can therefore be classed as lignin-modifying enzymes. Other laccases produced by fungi can facilitate the biosynthesis of melanin pigments. Laccases catalyze ring cleavage of aromatic compounds.

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.

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Frank Neese is a German theoretical chemist at the Max Planck Institute for Coal Research. He is the author of more than 440 scientific articles in journals of Chemistry, Biochemistry and Physics. His work focuses on the theory of magnetic spectroscopies and their experimental and theoretical application, local pair natural orbital correlation theories, spectroscopy oriented configuration interaction, electronic and geometric structure and reactivity of transition metal complexes and metalloenzymes. He is lead author of the ORCA quantum chemistry computer program. His methods have been applied to a range of problems in coordination chemistry, homogeneous catalysis, and bioinorganic chemistry.

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<span class="mw-page-title-main">Transition metal thiolate complex</span>

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<span class="mw-page-title-main">Ben Feringa</span> Dutch Nobel laureate in chemistry

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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).

References

  1. 1 2 "National Academy of Sciences Member Directory - Edward I. Solomon". Archived from the original on 2019-03-24.
  2. 1 2 3 4 5 6 7 8 "Edward I. Solomon | Department of Chemistry". chemistry.stanford.edu. Retrieved 2021-05-17.
  3. "American Academy of Arts and Sciences - Edward Ira Solomon". Archived from the original on 2021-06-10.
  4. 1 2 3 Zagorski, N. (2006). "Profile of Edward I. Solomon". Proceedings of the National Academy of Sciences. 103 (35): 12963–12965. Bibcode:2006PNAS..10312963Z. doi: 10.1073/pnas.0606007103 . PMC   1559735 . PMID   16924096.
  5. 1 2 3 Zagorski, Nick (2006-08-29). "Profile of Edward I. Solomon". Proceedings of the National Academy of Sciences. 103 (35): 12963–12965. Bibcode:2006PNAS..10312963Z. doi: 10.1073/pnas.0606007103 . ISSN   0027-8424. PMC   1559735 . PMID   16924096.
  6. Solomon, Edward I.; McClure, Donald S. (1972-09-01). "Jahn-Teller Effect in the $^{4}T_{1g}(I)$ State of ${\mathrm{Mn}}^{++}$ in RbMn${\mathrm{F}}_{3}$. II". Physical Review B. 6 (5): 1697–1708. doi:10.1103/PhysRevB.6.1697.
  7. Solomon, Edward I.; McClure, Donald S. (1974-06-01). "Comparison of the Jahn-Teller effect in four triply degenerate states of ${\mathrm{Mn}}^{++}$ in RbMn${\mathrm{F}}_{3}$". Physical Review B. 9 (11): 4690–4718. doi:10.1103/PhysRevB.9.4690.
  8. Solomon, Edward I.; Ballhausen, C. J. (1975-01-01). "Identification of the structure of the 3T1g (I) ← 3A2g band in the Ni(H2O)6 ++ complex". Molecular Physics. 29 (1): 279–299. doi:10.1080/00268977500100191. ISSN   0026-8976.
  9. Allendorf, M D; Spira, D J; Solomon, E I (1985). "Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site". Proceedings of the National Academy of Sciences of the United States of America. 82 (10): 3063–3067. Bibcode:1985PNAS...82.3063A. doi: 10.1073/pnas.82.10.3063 . ISSN   0027-8424. PMC   397714 . PMID   2987909.
  10. Wilcox, Dean E.; Porras, Arturo G.; Hwang, Yeong T.; Lerch, Konrad; Winkler, Marjorie E.; Solomon, Edward I. (1985). "Substrate analog binding to the coupled binuclear copper active site in tyrosinase". Journal of the American Chemical Society. 107 (13): 4015–4027. doi:10.1021/ja00299a043. ISSN   0002-7863.
  11. Allendorf, M. D.; Spira, D. J.; Solomon, E. I. (1985-05-01). "Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site". Proceedings of the National Academy of Sciences. 82 (10): 3063–3067. Bibcode:1985PNAS...82.3063A. doi: 10.1073/pnas.82.10.3063 . ISSN   0027-8424. PMC   397714 . PMID   2987909.
  12. Glaser, Thorsten; Hedman, Britt; Hodgson, Keith O.; Solomon, Edward I. (2000-12-01). "Ligand K-Edge X-ray Absorption Spectroscopy: A Direct Probe of Ligand−Metal Covalency". Accounts of Chemical Research. 33 (12): 859–868. doi:10.1021/ar990125c. ISSN   0001-4842. PMID   11123885.
  13. Wang, Linda. "Alfred Bader Award In Bioinorganic Or Bioorganic Chemistry: Edward I. Solomon | Chemical & Engineering News". cen.acs.org. Retrieved 2016-10-09.
  14. "Faculty | Department of Chemistry". Archived from the original on 2015-05-11. Retrieved 2015-05-08.