xt7cfx73xr51 https://exploreuk.uky.edu/dips/xt7cfx73xr51/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 19940411 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 Twentieth Annual Symposium on Chemistry and Molecular Biology: "Nitrogenase: The Chemistry of Biological Nitrogen Fixation" text Twentieth Annual Symposium on Chemistry and Molecular Biology: "Nitrogenase: The Chemistry of Biological Nitrogen Fixation" 1994 2017 true xt7cfx73xr51 section xt7cfx73xr51 m
1994 PROGRAM Twentieth Annual
—_ — __’— ‘ Symposium on
AM. P.M.
9:00 Registration and Coffee - Room 137. 12:15 Buffet Lunch, Faculty Club (Please return 0
Chemistry-Physics Building card by April 1, 1994 for reservations. Chemlstry
9:30 Wecome by Dr. David Watt, Vice Chancellor COSt $1000 to be paid at registration.)
fonResearch and Graduate Studies, 1:40 Dr. Robert R. Eady, University of Sussex
Umversrty of Kentucky - Room 139. . . . .
Ch , t Ph , B ,1 d‘ The Role of Vanadium in Biological
emls ry- ys1cs “1 mg Nitrogen Fixation
9:40 Introductory Remarks - Mark Meier.
University of Kentucky Three related, but genetically distinct. nitrogenase l
_ _ _ . systems are known to be present in Azotobacter species. 0 e c ‘1 ar
9'45 Dr. Douglas C' Rees, California Institute Of One. which is found in all Ng—fixing bacteria and has been
Technology _ . studied extensively for many years, is based on Q
The Structure and Function ofNitrogenase molybdenum and iron: at second [first isolated in 1986) B1010
The conversion of dinitrogen to ammonia during contains vanadium and ironzandathird (first isolated in
biological nitrogen fixation is catalyzed by the nitro- 1988] appears to contain only iron. Which of these
genase enzyme system. Nitrogenase consists of two systems 18 expressed depends on the avallability of
component proteins, the iron [Fe—) protein and the Mo and V to the organism. The results of studies on the
molybdenum—iron [MoFe—) protein. Three—dimensional regulation of the expression of these alternative systems ,
structures of both proteins have been determined by by M0 and V and the structure—function relationships of
X—ray crystallography. The MoFe—protein is an 05232 V-nitrogenase. in comparison with Mo—nitrogenase 0f
tetramer containing two different types of metal centers. Azotobacter WI” be rev1ewed. ' ‘ '
the FeMo—cofactor and the P-cluster pair. while the . .
Fe-protein contains a single 4Fcz4S cluster symmetri— 2:40 Discussron .
cally ligated by two identical subunits. Aspects of the . . _ . . . _ ,
n’itrogenase mechanism. as well as general structural 250 D1." D3m‘tn Coucouvanls, UniverSIty 0f
similarities that exist between nitrogenase and other Michigan ‘ ‘ t bl' h d . th f
complex electron transfer systems, will be explored. :yntlletlc Models ofthe Nitrogenase Fe/Mo/S CS a IS 6 In 6 memory 0
us er :
10:45 Discussion Anna A' Naff
1055 Dr William E Newton Vir inia Recent X—ray structure determinations of the Fe/Mo
' Pol tech nic and State’UniEersit protein of nitrogenase revealed the structure of the _————_‘—_———
ProSI’n'ng Ni trogenase Catalytic FYunction Fe / Mo / S active site. Neither the Fe453 nor the MoFe383 NITROGEN ASE;
. . . . subunits have precedents among synthetic clusters with
Through Ammo Add Substitutions biologically acceptable terminal ligands. In this lecture THE CHEMISTRY OF BIOLOGICAL
The nitrogenase complex consistsof a smaller Fe we will report on the first observation of catalytic NITROGEN FIXATION
protein.which acts as an ATP—binding, specific electron behavior by synthetic Fe/MO/S clusters that struc— E” B
donor to the larger 0.3133 MoFe protein, which contains turally. albeit partially. resemble the Fe/MO/S site of 4—! 8 __—————
the substrate—binding site. The MoFe protein contains nitrogenase. Some of these clusters are effective in the .‘2 E“ |
two types of prosthetic group: two P—cluster pairs, each catalytic reduction 0f hydrazine to ammonia in what E g 8 SPEAKERS
ofwhich consists oftwo [4Fe—4S] clusters bridged by the COUld be the 1351 stage in nitrogen fixation. Reactivity .: *4 L0 , , , _
y»S of two cysteinyls (Cys) and a likely disulfide bond: studies strongly implicate the Mo atom as the site directly 0 E g D1rn1tr1 N. COUCOleal’llS
and two FeMo-cofactors {or M centers), each of which involved in the reduction of N3H4. These studies also ‘8 M Robert R_ Eady
has the composition, MoFe7S.){homocitrate). Our ap- suggest that the catalytic process likely occurs by a H ‘45 E . _
proach to assigning function to the individual prosthetic single metal site mechanism. POSSible pathways Of these 8 3‘ 52‘: Wllham E- NCWtOI’I
groups is through site—directed mutagenesis/gene- reactions will be presented E 7) 8 Douglas C. Rees
replacement techniques, then monitoring the conse— t: 3-; no
quences of these substitutions. Correlated changes in 3150 Discussion a 3 E
EPR spectra and catalytic properties occur on substitu— q; 3:: Monda A til 1 1 1994
tion of residues interacting with the FeMo cofactor, 4:00 Mixer - Room 137, Chemistry-Physics D D .3 Y, P ’
indicating the intimate involvement of this prosthetic Building
group with the substrate—reducing site. Aworking model -
ofnitrogenase function based on these and other results DEpEirtmdl’lt Of ChemlStry
will be described. Un1vers1ty of Kentucky
11:55 Discussion Lexington, Kentucky 40506—0055

 I I
Twentieth Annual Symposmm on
Ch e mistr y &
Molecular Biology
established 1n the memory of Anna S. Naff
Monday April 1 1, 1994 9:00 am.
Room 1 39, Chemistry—Physms Buildlng
Department of Chemlstry, Univer51ty of Kentucky
m- , m w
Dimitri N. Coucouvanis, Professor of Chemistry, Univer- Robert R. Eady, Senior Principal Research Fellow in the
sity of Michigan. PhD. Case Institute of ’l‘echnology: AFRC Nitrogen Fixation Laboratory at The University of
Postdoctoral Fellow, Columbia University. Alfred P. Sloan Sussex, England. Ph.D. D.Sc. The University of Hull.
Fellow; Guggenheim Fellow; Willsmore Fellow (Melbourne), England: Joined the staff of the AF RC Unit of Nitrogen
MorelyAward (Cleveland ACS): Distinguished FacultyAchieve— Fixation (latterly the AFRC Nitrogen Fixation Laboratory) in
ment Award (University of Michigan): Editorial Boards. 1969; Individual Merit research appointment (1989);
Inorganic Chemistry and Polyhedron. Biochemical Society visitor to Australia: Course tutor in
Microbiology, the Pasteur Institute (Paris, France); Course
tutor: EEC—European Science Foundation Advanced Course
‘Chemistry of Metals in Biological Systems” (Louvain—
1aNeuve. Belgium); Honourary lecturer in Biochemistry, The
University of Sussex.
Douglas C. Rees, Professor of Chemistry, California Insti- William E. Newton, Professor of Biochemistry, Virginia
tute of Technology. Ph.D. Harvard University (W .N. Lipscomb, Polytechnic and State University. Ph.D., University of
thesis advisor]; Postdoctoral Fellow, Harvard University and London; Chairman, International Steering Committee for the
University of Minnesota. Current Advisory Boards: Science: International Congresses on Nitrogen Fixation.
Protein Science. (photo credit: Bob Paz/CalTech)
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 additional information. call Mark Meier. Department of Chemistry.
(606] 257—3837.
1994 Committee: Mark S. Meier (Co—chair], John P. Selegue (Co—chair), Vahid Majidi, Sylvia Daunert
Symposium supported by the Anna S. Naff Endowment Fund