xt7vt43j179m https://exploreuk.uky.edu/dips/xt7vt43j179m/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 20120504 A brochure for the Naff Symposium, an event hosted by the University of Kentucky Chemistry Department supported by the Anna S. Naff Endowment Fund. This brochure belongs to the University of Kentucky Chemistry Department Records collection, accession number 2014ua075. archival material  English University of Kentucky Chemistry Department Contact the Special Collections Research Center for information regarding rights and use of this collection. University of Kentucky Chemistry Department Naff Symposium brochures Thirty-Eighth Annual Symposium on Chemistry and Molecular Biology: "Metals and Proteins" text Thirty-Eighth Annual Symposium on Chemistry and Molecular Biology: "Metals and Proteins" 2012 2017 true xt7vt43j179m section xt7vt43j179m _“
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2012 PROGRAM . 8 ThIrty Elghth Annual
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8:00 a.m. Registration & Continental Breakfast doxin family that are involved in long-range electron transfers fig 9 Q g .
Keeneland Room, W.T. Young Library in many important biological processes such as photosynthe- 2 a? < c“ r: C hem Istry
8:50 a.m. Welcome —— Dr. Eli Capilouto sis, to span ~1 V through carefully design of hydrophobicity ‘5 vi “- fig
President, University of Kentucky and hydrogen bonding networks around the primary coordi- d; D .5 r1 &
9:00 a.m. Dr. Brian Crane nation sphere, and the use of these redox proteins to ad- 8 3.
Cornell University dress fundamental questions in biological electron transfers 2 M I I
How Metal, Nitric Oxide and Redox Chemistry such as reorganization energy and Marcus inverted region. In 0 ecu ar
Coordinate Cellular Responses in Microbes the second example, we have shown that the roles of two .
and Men conserved glutamate in converting myoglobin into nitric oxide B I Ology
reductase, one through binding to a non-heme iron and the
Nitric oxide (NO) is a small, reactive and diffusible agent other through hydrogen bonding interaction. Finally, we pre-
produced by the complex redox chemistry of the nitric ox- sent recent unpublished results that the presence of waters \. \
ide synthases (NOSs). In mammals, NOSs generate NO as part of a new hydrogen-bonding network in myoglobin is / '
as a second messenger for many purposes that include necessary to confer oxidase activity in reducing 02 to water _ l
' neuronal transmission, regulation of the vasculature and with minimum release of other reactive oxygen species and
release of hormones. In addition, immune cells produce with > 1,000 turnovers. //
NO as part of the oxidative burst to combat pathogens and I / V
tumor cells. Microbial NOSs are less understood but ap- 11:30 a.m. Lunch l
pear to involve NO in novel mechanisms that include toxin 1:30 pm. Poster Session, Gallery, W.T. Young Library «
biosynthesis, protection against oxidative damage and the 2:30 pm. Dr. Harry Gray
coordination of stress responses. A common theme in this California Institute of Technology .
broad spectrum of reactivity is the ability of NO to mediate Electron Flow through Metalloproteins Es,tab“3hed by M' Benton Naff
redox reactions at metalloenzyme centers. The chemistry in memory 0f Anna 3- Naff
‘ of NO production and targeting will be discussed as well as Electron transfers in photosynthesis and respiration common-
emerging roles of this fascinating molecule. ly occur between metal-containing cofactors that are separat- . —_
ed by large molecular distances. Understanding the underly- -
10:00 a.m. Break (refreshments available) ing physics and chemistry of these biological electron trans- D m
10:30 a.m. Dr. Yi Lu fer processes is the goal of much of the work in my laborato- Ln UJ
University of Illinois at Urbana-Champaign ry. Employing laser flash-quench triggering methods, we 3‘ 8 '—
Designing Functional Metalloproteins: have shown that 2—nm, coupling-limited Fe(|l) to Ru(l|l) and E >,C.> a ' SPEAKERS
Exploring the Roles of Non-covalent Cu(l) to Ru(l|l) electron tunneling in Ru-modified cyto- E 6 8 3
Interactions in Conferring and Fine-tuning chromes and blue copper proteins can occur on the micro- g 3 L0 0 ,
Enzymatic Activities second timescale both in solutions and crystals. Redox o g g [5&1 Dr- Br'an Crane
. equivalents can be transferred even longer distances by mul- ~45 g >_ Dr_ Yi Lu
,Designing metalloproteins is an ultimate test of our tistep tunneling (hopping) through intervening tyrosines and H H— x ”J
. . o 0 Dr. Harry Gray
knowledge about metalloproteins and can result In new tryptophans. In recent work, we have found that 2— to 3-nm g > c" S
biocatalysts for practical applications. In this presentation, hole hopping through one or more intervening tryptophans is E *5 9 m
we provide three examples to demonstrate that, while re- several orders of magnitude faster than single-step tunneling t’ 5 U) LIJ
producing the primary coordination sphere may be good in Re—modified mutants of Pseudomonas aeruginosa azurin. 82 ->E< ‘0 Frid M 4th 2012
enough to make structural models of metalloproteins, care- The lessons we have learned about the control of electron 0) C a) ‘0 ay’ ay ’
ful design of the non-covalent secondary coordination tunneling and hopping are now guiding the design and con- D D —' fl
sphere interactions is required to create functional metallo- struction of sensitizer—modified redox metalloenzymes and n: .
proteins. In the first example, we demonstrate the fine- other molecular machines for the production of fuels and z D Department Of Chem'Stry
tuning of reduction potentials of azurin a member of cupre- oxygenated hydrocarbons from sunlight and water. = 2 University Of Kentucky
Lexington, KY 40506-0055
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 - The Department of Chemistry, UniverSIty of Kentucky
' ; presents the
Thirty-Eighth Annual Symposmm on
C h e m istry &
Molecular Biology
Established by M. Benton Naff in memory of Anna S. Naff
Friday, May 4*“, 2012 9:00 am.
- “MW?“ Auditorium, William T. Young Library
- Metals and Proteins
_ ’ ‘ , 2‘11“”??{7299' ! Brian Crane is a professor of Chemistry and Chemical Biology at Cornell University.
. _~ -,\/ g . ‘ He received his BS. degree from the University of Manitoba and his PhD. from the Scripps
‘ ~ , . ’g , Research Institute under Dr. Elizabeth Getzoff. After a short postdoctoral stay with Dr. John _
35" ‘ ‘ ' a Tainer at Scripps, he trained with Prof. Harry Gray at Caltech as a Helen Hay Whitney Post-
‘ ~ ,5 w .~ -. ,"“"‘ doctoral Fellow. Crane studies protein structure and enzymatic mechanism in systems where
.w. ‘9; j 4.; redox chemistry, photochemistry and cooperative macromolecular interactions are important
' .. .' s s: . fly.“ for cellular function. His specific interests include nitric oxide enzymology, light sensors and
:Qg‘tfi, .1. ”*5. oscillators of circadian clocks and the sensory apparatus that mediates bacterial chemotaxis.
' %’ t~ j- “it For this work he has been named a Fellow of the American Association of Arts and Sciences,
j" 2‘ i. 'f' .9 an Alfred P. Sloan Fellow, and a Searle Scholar. He has received awards that include a Drey-
&, § X,‘ .: fus New Faculty Award, a Research Innovation Award and most recently, the Cornell Provost
‘ S ‘: Award for Research and Scholarship.
Yi Lu is the Jay and Ann Schenck Professor of Chemistry at the University of Illinois
at Urbana-Champaign. He received his BS. degree from Peking University in 1986, and
PhD. degree from University of California at Los Angeles in 1992 under Professor Joan S.
Valentine. After two years of postdoctoral research in Professor Harry B. Gray‘s group at the
> ., - . California Institute of Technology, Dr. Lu started his own independent career in the Depart—
‘T‘MT'T'T'W 3‘ T“: ' ment of Chemistry at the University of Illinois at Urbana—Champaign in 1994. He is now the
.» ._ ‘X Jay and Ann Schenck Endowed Professor of Chemistry and HHMI Professor in the Depart—
ments of Chemistry, Biochemistry, Bioengineering and Materials Science and Engineering.
a He is also a member of the Center for Biophysics and Computational Biology and the Beck-
1 ‘ man Institute for Advanced Science and Technology. His research interests lie at the inter-
, ‘ face between chemistry and biology. His group is developing new chemical approaches to
' I provide deeper insight into biological systems. At the same time, they take advantage of
,_ ‘=. recently developed biological tools to advance many areas in chemistry. Specific areas of
current interests include a) design and engineering of functional metalloproteins as environ-
* mentally benign catalysts in renewable energy generation and pharmaceuticals; b) Funda—
mental understanding of DNAzymes and their applications in environmental monitoring, medical diagnostics, and target—
ed drug delivery; and c) Employing principles from biology for directed assembly of nanomaterials and its applications in
photonics and sensing. Dr. Lu has received numerous research and teaching awards, including the Fellow of the Ameri—
can Association for the Advancement of Science (2007), Early Career Award, Society of Biological Inorganic Chemistry
(2007), Howard Hughes Medical Institute Professor Award (2002), Camile Dreyfus Teacher-Scholar Award (1999), AI—
fred P. Sloan Research Fellowship (1998), Research Corporation Cottrell Scholars Award (1997), and the Beckman
Young Investigators Award (1996).
. E. " ., . Harry Gray is the Arnold O. Beckman Professor of Chemistry and the Founding Direc-
‘ 1’» ~. 3;. ’ . ,“ tor of the Beckman Institute at the California Institute of Technology. He received his
.‘3 EM V- _. _‘ )3 BS. degree from Western Kentucky University in 1957. After graduate work at Northwest-
5 rh- _;_( Ligfifga ern University and postdoctoral research at the University of Copenhagen, he joined the
. é 4* Xi ‘11. chemistry faculty at Columbia University, where in the early 1960s he developed ligand field
., gr. ' theory to interpret the electronic structures and substitution reactions of metal complexes.
’1 After moving to Caltech in 1966, he began work in biological inorganic chemistry and solar
J photochemistry, including the development of inorganic systems for energy storage. Work-
' ' “"“"“"“ "“’ " “ ‘ ing With Ru-modified proteins in the early 19805, he demonstrated that electrons can tunnel
rapidly over long molecular distances through folded polypeptide structures; and, in the
years following, he and J. R. Winkler developed laser flash-quench methods that opened the
, way for experimental investigations that have led to a deeper understanding of the mecha—
' ‘ - nisms of electron flow through proteins that function in respiration and photosynthesis. Dr.
Gray has published over 800 research papers and 18 books. He has received the National Medal of Science from Pres-
ident Ronald Reagan (1986); the Pauling Medal (1986); the Linderstrom-Lang Prize (1992); the Gibbs Medal (1992);
the Harvey Prize (2000); the National Academy of Sciences Award in Chemical Sciences (2003); the Benjamin Franklin
Medal in Chemistry (2004); the Wolf Prize in Chemistry (2004); the City of Florence Prize in Molecular Sciences (2006);
the Welch Award(2009), the Priestley Medal (1991); and 16 honorary doctorates, including ones from Rochester, North-
western, Pennsylvania, Chicago, Columbia, Toulouse, Florence, Copenhagen, and Edinburgh. He is a member of the
National Academy of Sciences; the American Academy of Arts and Sciences; the American Philosophical Society; a
foreign member of the Royal Danish Academy of Sciences and Letters; the Royal Swedish Academy of Sciences; the
Royal Society of Great Britain; and the Accademia Nazionale dei Lincei. He has been a member of the Board of Direc-
tors of the Arnold and Mabel Beckman Foundation since 1994.
For additional information, contact Professor Edith Glazer, Department of Chemistry, ec.g|azer@uky.edu.
2012 Committee: Professor Edith Glazer (Chair, Chemistry), Professor Jason DeRouchey (Chemistry),
Professor Mark Watson (Chemistry), Professor Anne-Frances Miller, Dean Tim Tracy (College of Pharmacy)
Symposium supported by the Anna S. Naff Endowment Fund