This biographical article is written like a résumé .(September 2021) |
Edward I. Solomon | |
---|---|
Born | Edward Ira Solomon 1946 (age 77–78) |
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 advisors | Carl J. Ballhausen, Harry B. Gray |
Doctoral students | Serena DeBeer, Darlene Joy Spira, Andrew Gewirth, Peng Chen, Daniel Gamelin, Abhishek Dey |
Other notable students | Frank Neese, Thomas Brunold, James Penner-Hahn |
Website | web |
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 been a longtime collaborator with many scientists, including his colleague at Stanford University Keith Hodgson for the study of metalloenzyme active sites by x-ray spectroscopy, along with the synthetic chemists Richard H. Holm, Stephen J. Lippard, Lawrence Que Jr. and Kenneth D. Karlin.
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]
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 the spectroscopic study of metal-containing enzymes involved in electron transfers and oxygen activation, and small molecules mimicking the active sites of these 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]
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.
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.
Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts. Both Complex I and Complex II of oxidative phosphorylation have multiple Fe–S clusters. They have many other functions including catalysis as illustrated by aconitase, generation of radicals as illustrated by SAM-dependent enzymes, and as sulfur donors in the biosynthesis of lipoic acid and biotin. Additionally, some Fe–S proteins regulate gene expression. Fe–S proteins are vulnerable to attack by biogenic nitric oxide, forming dinitrosyl iron complexes. In most Fe–S proteins, the terminal ligands on Fe are thiolate, but exceptions exist.
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.
In enzymology, a bilirubin oxidase, BOD or BOx, (EC 1.3.3.5) is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction
Christopher David Garner FRSC FRS is a British retired chemist, whose research work was in the growing field of Biological Inorganic Chemistry. His research primarily focussed on the role of transition metal elements in biological processes, for which he published over 400 original papers and reviews on the topic. His specific interests lie in the roles of Molybdenum and Tungsten as the metal centres in various enzyme cofactors based on the molybdopterin molecule.
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