xt7ffb4wm34q https://exploreuk.uky.edu/dips/xt7ffb4wm34q/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 19870424 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 Thirteenth Annual Symposium on Chemistry and Molecular Biology: "Electron Transfer in Metalloproteins" text Thirteenth Annual Symposium on Chemistry and Molecular Biology: "Electron Transfer in Metalloproteins" 1987 2017 true xt7ffb4wm34q section xt7ffb4wm34q 1987 PROGRAM ’3? g' B
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P M :3 E g Thirteenth Annual Symposrum on
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12:15 Buffet Lunch Faculty Club 3: Ha
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9 00 RSI-gislggtion and 0 98 em stry ysics (Please return card by April 15, 1987 for M: 7: 9"
‘ reservation. Cost $6.00 to be paid at 4: g 0
9:30 Welcome by Dean Wimberly C. Royster registration.) O "" :T‘ .
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Vice-Chancellor for Research. University of g 0 3 Che ISt and
Kentucky Chemistry Physics Rm 139 1:30 Dr. Harry B. Gray. California Institute of CN 5 __,, .
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Technology a s: Molecular Biology
9:35 Introductory Remarks Long-Range Electron Transfer in Heme Q \C
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9:40 Dr. George McLendon, University of ro e ns 0'!
Rochester Kinetic experiments at Northwestern, Rochester, Brookhaven, , . ,
Birds Do It, Bees Do It: How Does Biology and Caltech have conclusively shown that electrons can be transfer- / , . , I,
Transport Electrons? red relatively rapidly over large distances (greater than 10 , , , , , f _ 5, .» ._
Biological energy is channeled via a series of simple electron angstroms) in proteins. Current research focuses on the factors established 111' the memory "of
transfer reactions. A brief overview will be presented of how elec- :Zhggzrmlgetdii: it: 022:: long-ralnge eleEtron transfters m ( Anna S . Naff
tron transfer occurs over long distances in simple chemical systems. th . p dtf. d I: b' cgmr: EXES' xpherrmen S on , ,, f , . ,
This work demonstrates that electron transfer reactions can occur n; tehnrumimo ll: {“on O '35 :n W 0C rotmest av: examrnc; "
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rapidly (<1065 1) even when the reactants do not collide and are e et'ro es Th ‘5 arlce a‘nth’ one; aficep :r 5 “fl: Lires an ‘
widely separated (eg 15 A). The recent results fully support the (grease 1C: ZZfererdifdons. 15 wor a: ll OW; t: are em ELECTRON TR NSFER
-r d' t' d b M d H 1" 1d t' ‘ e cron- ra ecrease exponen 1a y W] e omr» ,_ . . A
F e 1C ions ma 2 y arcus an op 1e some rme ago acceptor edge-to-edge distance. Evidence that an intervening , ' .
10:40 Break aromatic residue enhances long-range donor-acceptor electronic , I
1050 Dr William H Orme-Johnson coupling has been obtained in studies of electron transfer from ‘ IN ,
' ' Massachusetts. Institute of Tedhnolo the excited triplet state of a zinc porphyrin to a ruthenium accep-
Electron Transfer and Biolo ical Nita: en tor in a doubly substituted myoglobin. Recent work involving METALLOPROTEINS
Fixation g g systematic variations in donor-acceptor energetics has defined ex- , , L, ’
In organisms that can utilize metabolic energy derived from car perimentally the reorganization energies for protein electron *
‘ transfer , ' .
bohydrate metabolism to carry out the reduction of atmospheric “ f '
nitrogen to ammonia, a specialized set of enzymes oxidizes 2:30 Break S k . . ‘ .
pyruvate and conveys to dinitrogen the reducing equivalents thus 240 Dr. Brian M Hoffman Northwestern pea ers , g '
obtained. Through the four proteins participating directly in this University ’ 7‘1" 9 ' f f
process, the eight electrons ultimately used during the reduction Long-Range Electron Transfer Between HARRY B GRAY
of one N2 molecule are passed one at a time. For the case of the Pr / ,. , . - . ,
oteins ,
free-living nitrogen fixer Klebsiella pneumoniae, an essentially com- W _ th t h . f t l l t 'th' BRIAN M HOFFMAN
plete genetic analysis suggests that seventeen genes are required h epfgee‘usr:g t : efclonrque 0 (me 252?; alceinent WI :1“ GEORGE MCLENDQN
to synthesize and regulate the components of the nitrogen fixa~ , emo ins O S u y 0 rig-range cat e ec ro-n- unne _ “ ”f I _
tion system. Using the tools of genetic engineering as well as spec» ing in protein complexes that incorporate redox centers rigidly held WILLIAM H ORME JOHNSON
troscopic procedures the nature of the prosthetic groups required fixed at crystallographically known distance and orientation. One
for electron transfer and the chemistry they catalyze is being ex- system we emplohy rs thimledc‘lmétfil hyrrrddhefrjnfiglobin; hav- '_
plored. Novel features of this complex system, perhaps of more lnhg onefype o C Iarrtrhsu :trtréem thb adc 0159 dsd‘: meta of“:
general significance, include the use of metal centers to do the Eh yrrn, orlexargr: e e [ nt’ eh ] y r1 5. :la 'tloln’ :efiL: 2; ,
2e'/le' transformer separation normally carried out by flavins, the :2 cromp ex e wee: cy 9C “ET“: 2 an ”(1: a Hsu S l ”,5 Monday: Apnl 24! 1987
utilization of a low molecular weight protein electron carrier cy OC rome E peroxr ase, m w lc case we irec y mom or De artment of Chemistr-
long-range intermolecular electron transfer between roteins that p y
(flavodoxin) operating at nearly diffusion - controlled rates. the l d W f‘ d h _ , .p h , U . t f K t k
coupling of MgATP hydrolysis to low potential electron transfer, are natilrra reh ox pafrtners. H e in t at varratronsbin t ecriaroterg nrversr y 0 en LlC y
and the accumulation of multiple elections in 19' storage sites in matrixt roug use 0 natura y occumng variants or y srte- rrecte r‘ 02 Lexington, Kentucky 40506-0055
the Nz-reducing component mutagenesrs can dramatically alter electron transfer rates. v 3 :3
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11:50 Discussion 3:40 Discussion a E 'v E: g?
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4:00 Social Hour, Chemistry-Physics, Rm. 137 g p: 5'- g .30
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We encourage symposium participants, especially students, to E 22;.
take this opportunity to meet with the speakers. =

 Thirteenth Annual Symposium on
Chemistry and Molecular Biology
established in the memory of Anna S. Naff
Monday, April 24, 1987 9:00 am.
Chemistry-Physics Building—Rm. 139
Department of Chemistry University of Kentucky
_
—
Harry B. Gray, Ph.D. Chemistry, 1986 Reci- George McLendon, PhD. Inorganic
pient of the Pauling Medal and the National Chemistry, 1987 American Chemistry Society
Medal of Science. Member of the National ' AWard in Pure Chemistry, AP. Sloan Fellow,
Academy of Sciences. Arnold O. Beckman Pro- Dreyfus Teacher—Scholar. Professor of
fessor of Chemistry and Director of the Beckman Chemistry, University of Rochester. Topic:
Institute at the California Institute of Technology. “Birds Do It, Bees Do It: How Does Biology
Topic: “Long-Range Electron Transfer in Heme Transport Electrons?”
Proteins”.
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Brian M. Hoffman, Ph.D. Chemistry, Alfred William H. Orme-Johnson, PhD. Chemistry,
P. Sloan Fellow, NIH Career Development PHS Career Development Awardee, l. H.
Award, E. Leon Watkins Visiting Professor, Romnes Faculty Fellow, Fellow of the American
Fellow of the American Association for the Ad- Association for the Advancement of Science.
vancement of Science. Professor of Chemistry Professor of Chemistry, Massachusetts Institute
and of Biochemistry, Northwestern University. of Technology. Topic: “Electron Transfer and
Topic: “Long-Range Electron Transfer Between Biological Nitrogen Fixation.” _
Proteins.”
Parking available free at Commonwealth Stadium on Cooper Drive. Shuttle buses run to the main campus. Additional parking
(for a fee) available in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry-Physics
Building; this garage can be accessed from both Rose and Limestone Streets—look for Medical Plaza Parking signs. For addi-
tional information, contact Prof. John P. Selegue, Dept. of Chemistry, 606—257-4741.
Symposium supported by the Anna S.,Naff Endowment Fund.