Harry B. Gray

Last updated
Harry Gray
Harry Gray HD2013 Othmer Gold Medal 002.JPG
Gray in 2013
Born
Harry Barkus Gray

(1935-11-14) November 14, 1935 (age 88)
Alma mater Western Kentucky University B.S. (1957) [1]
Northwestern University Ph.D, D.Sc. (1960)
Known for Bioinorganic Chemistry
Electron Transfer chemistry
Photochemistry
Awards ACS Award in Pure Chemistry (1970)
Tolman Award (1979)
National Medal of Science (1986)
AIC Gold Medal (1990)
Priestley Medal (1991)
Harvey Prize (2000)
William H. Nichols Medal (2003)
Wolf Prize in Chemistry (2004)
Welch Award (2009)
Othmer Gold Medal (2013)
Scientific career
Fields Chemistry
Institutions Columbia University
California Institute of Technology
Doctoral advisor Fred Basolo, Ralph Pearson
Doctoral students
Other notable studentsUndergrads:Post-docs:
Website www.cce.caltech.edu/content/harry-b-gray
External videos
Beckman Institute Reflection.jpg
Nuvola apps kaboodle.svg Harry Gray discusses How Arnold O. Beckman's Instrumental Voice Shaped Chemistry's History, and the Beckman Institute at Caltech; Profiles in Chemistry, Chemical Heritage Foundation

Harry Barkus Gray (born November 14, 1935) is the Arnold O. Beckman Professor of Chemistry at California Institute of Technology. [2]

Contents

Career

Gray received his B.S. in chemistry from Western Kentucky University in 1957. He began his work in inorganic chemistry at Northwestern University, where he earned his Ph.D. in 1960 working under Fred Basolo and Ralph Pearson. He was initiated into the Upsilon chapter of Alpha Chi Sigma at Northwestern University in 1958. [3] After that, he spent a year (1960–61) as an NSF Postdoctoral Fellow at the University of Copenhagen, [4] where, along with Walter A. Manch, he collaborated with Carl J. Ballhausen on studies of the electronic structures of metal complexes. [5] [6]

After completing his NSF Postdoctoral Fellow at the University of Copenhagen, he relocated to New York City to take up a faculty appointment at Columbia University. He served as an assistant professor from 1961 to 1963 and as an associate professor from 1963 to 1965.

In 1966, he became the Arnold O. Beckman Professor of Chemistry at California Institute of Technology, and founding director of the Beckman Institute for Advanced Science and Technology. [7] He also served on the Physical Sciences jury for the Infosys Prize from 2010 to 2013.

Gray also trained future leaders of several major science research universities. Four of his doctoral students became presidents or chancellors of University of Rhode Island, Iowa State University, University of North Carolina at Chapel Hill, and Washington University in St. Louis. [8]

Research

Gray's interdisciplinary research program addresses a wide range of fundamental problems in inorganic chemistry, biochemistry, and biophysics. Electron transfer (ET) chemistry is a unifying theme for much of this research. [9]

Over the past twenty-five years the Gray group has been measuring the kinetics of long-range ET reactions in metalloproteins labeled with inorganic redox reagents. Early research by his lab members showed that details of the internal structures of the proteins dominate the ET rates. [10] Current research is aimed at understanding how intermediate protein radicals accelerate long-range ET. In collaboration with Jay R. Winkler of the Beckman Institute at Caltech they have developed new techniques for measuring ET rates in crystals of Ru-, Os-, and Re-modified azurins, as well as crystals of Fe(III)-cytochrome c doped with Zn(II)-cytochrome c. [11] This method of integrating photosensitizers into protein crystals has provided a powerful new tool for studying biochemical reaction dynamics. [12] The Gray/Winkler group is also using ET chemistry to probe the dynamics of protein folding in cytochrome c. [13]

Major publications

Awards and honors

His accolades include:

Wolf Prize

He was awarded the Wolf Prize in Chemistry in 2004 for his pioneering work in bioinorganic chemistry, unraveling novel principles of structure and long-range electron transfer in proteins. [9] [27]

Gray has made generative contributions to the understanding of chemical bonding of metal complexes, mechanisms of inorganic reactions, spectroscopy and magneto-chemistry of inorganic compounds. His study of the first trigonal prismatic complexes is one such example. Harry Gray's most significant work lies at the interface between chemistry and biology. As a pioneer of the important and thriving field of bioinorganic chemistry, he has made many key contributions, the most important of which is the development of fundamental understanding of electron transfer in biological systems, at the atomic level. [28]

Related Research Articles

<span class="mw-page-title-main">Cytochrome c</span> Protein-coding gene in the species Homo sapiens

The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion where it plays a critical role in cellular respiration. It transfers electrons between Complexes III and IV. Cytochrome c is highly water-soluble, unlike other cytochromes. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It also plays a major role in cell apoptosis. In humans, cytochrome c is encoded by the CYCS gene.

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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.

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Christopher J. Chang is a professor of chemistry and of molecular and cell biology at the University of California, Berkeley, where he holds the Class of 1942 Chair. Chang is also a member of the Helen Wills Neuroscience Institute, a Howard Hughes Medical Institute investigator, adjunct professor of pharmaceutical chemistry at the University of California, San Francisco, and faculty scientist at the chemical sciences division of Lawrence Berkeley Lab. He is the recipient of several awards for his research in bioinorganic chemistry, molecular and chemical biology.

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

A transition metal oxo complex is a coordination complex containing an oxo ligand. Formally O2-, an oxo ligand can be bound to one or more metal centers, i.e. it can exist as a terminal or (most commonly) as bridging ligands (Fig. 1). Oxo ligands stabilize high oxidation states of a metal. They are also found in several metalloproteins, for example in molybdenum cofactors and in many iron-containing enzymes. One of the earliest synthetic compounds to incorporate an oxo ligand is potassium ferrate (K2FeO4), which was likely prepared by Georg E. Stahl in 1702.

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Frances Ann Walker was an American chemist known for her work on heme protein chemistry. She was an elected fellow of the American Association for the Advancement of Science and the American Chemical Society.

References

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  5. Avery, John; Dahl, Jens Peder; Hansen, Aage E. (1987). Understanding Molecular Properties a Symposium in Honour of Professor Carl Johan Ballhausen, held at The Royal Danish Academy of Sciences and Letters, April 4 and 5, 1986. Dordrecht: Springer Netherlands. pp. ix–x. ISBN   978-94-009-3781-9 . Retrieved October 25, 2016.
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  10. Beratan, DN; Betts, JN; Onuchic, JN; et al. (1991). "Protein electron transfer rates set by the bridging secondary and tertiary structure". Science. Sciencemag.orgaccessdate=June 18, 2013. 252 (5010): 1285–8. Bibcode:1991Sci...252.1285B. doi:10.1126/science.1656523. PMID   1656523.
  11. Winkler, Jay R.; Gray, Harry B. (July 16, 2015). "Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?". Quarterly Reviews of Biophysics. 48 (4): 411–420. doi:10.1017/S0033583515000062. PMC   4793975 . PMID   26537399.
  12. Tezcan, F. Akif; Crane, Brian R.; Winkler, Jay R.; Gray, Harry B. (2001). "Electron Tunneling in Protein Crystals". Proceedings of the National Academy of Sciences of the United States of America. 98 (9): 5002–5006. Bibcode:2001PNAS...98.5002A. doi: 10.1073/pnas.081072898 . JSTOR   3055554. PMC   33153 . PMID   11296248.
  13. Mines, Gary A.; Pascher, Torbjörn; Lee, Sonny C.; Winkler, Jay R.; Gray, Harry B. (June 1996). "Cytochrome c folding triggered by electron transfer". Chemistry & Biology. 3 (6): 491–497. doi: 10.1016/S1074-5521(96)90097-6 . PMID   8807879.
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  28. Simply-Smart. "תוצאות חיפוש - פרס וולף". Wolffund.org.il. Retrieved February 14, 2015.