William N. Lanzilotta
Assistant Professor

A130 Life Sciences Building
Dept. of Biochemistry and Molecular Biology
University of Georgia
Athens, GA 30602-7668

706-542-1324 (office)
706-542-1573 (Lab)
706-542-1738 (fax)
wlanzilo@bmb.uga.edu

Research
Interests


Lab Members

Positions

Publications

Lecture Notes


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PUBLICATIONS: Reviewed

Medlock, A., Dailey, T. A., Ross, T. A., Dailey, H. A., and Lanzilotta, W. N. 2007 A pi-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase.
Journal of Molecular Biology 373(4) 1006-1016

Medlock, A., Swartz, L., Dailey, T. A., Dailey, H. A., and Lanzilotta, W. N. 2007 Substrate Interactions
With Human Ferrochelatase. P.N.A.S 104(6):1789-1793

Swartz, L., Kuchinskas, M., Li, H., Poulos, T. L., and Lanzilotta, W. N. 2006 Redox-Dependent
Structural Changes in the Azotobacter vinelandii Bacterioferritin: New Insights into the Iron
Transport Mechanism. Biochemistry 45(14), 4421-4428

Iyer RB, Silaghi-Dumitrescu R, Kurtz DM Jr, Lanzilotta WN. 2005 High-resolution
crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-
dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins.
J Biol Inorg Chem. 10(4), 407-416

Silaghi-Dumitrescu R, Kurtz DM Jr, Ljungdahl LG, Lanzilotta WN. 2005 X-ray crystal structures
of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a
scavenging nitric oxide reductase. Biochemistry 44(17):6492-6501.

O'Brien, J. R., Raynaud, C., Croux, C., Girbal, L., Soucaille, P., and Lanzilotta, W. N.
2004 Insight into the Mechanism of the B12-Independent Glycerol Dehydratase from
Clostridium butyricum
: Preliminary Biochemical and Structural Characterization.
Biochemistry (Accelerated Paper) 43, 4635-4645


O'Brien, J. R., Schuller D. J., Yang, V. S., Dillard, B. D., and Lanzilotta, W. N. 2003
Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate
dioxygenase and insight into the oligomeric structure. Biochemistry (Accelerated Paper)
42, 5547-5554

Chiu H., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C., Howard J.B.,
Rees D.C.. 2001 MgATP-Bound and nucleotide-free structures of a
nitrogenase protein complex between the Leu 127 Delta-Fe-protein and
the MoFe-protein. Biochemistry. 40, 641-50.

Shimizu, H., Schuller, D. J., Lanzilotta, W. N., Sundaramoorthy, M., Arciero, D.
., Hooper, A. B., and Poulos, T. L. 2001 Crystal Structure of Nitrosomonas
europaea Cytochrome c Peroxidase and the Structural Basis for ligand
Switching in Bacterial Di-heme Peroxidases. Biochemistry 40,
p. 13483-134901)

Thorsteinsson M.V., Kerby R.L., Conrad M., Youn H., Staples C.R., Lanzilotta
W.N., Poulos T.J., Serate J., Roberts G.P. 2000. Characterization of
variants altered at the N-terminal proline, a novel heme-axial ligand in
CooA, the CO-sensing transcriptional activator. J Biol Chem. 275,
39332-39338.

Lanzilotta, W. N., Schuller, D. J., Thorsteinsson, M. V., Kerby, R. L., Roberts,
G. P., and Poulos, T. L., 2000. Structure of the CO-sensing protein
from Rhodospirillium rubrim: Insight into the mechanism of allosteric
control in the CAP family of transcription factors. Nat. Struct. Bio.7, 876-880

Grunwald S. K., Ryle, M. J., Lanzilotta, W. N., Ludden, P. W. 2000. ADP
Ribosylation of varients of azotobacter vinelandii dinitrogenase
reductase-ridosyltransferase. J. Bacteriol. 182, 2597-260

Rangaraj, P., Ryle, M. J., Lanzilotta, W. N., Goodwin, P. J., Dean, D. R.,
Shah, V. K. 1999. Inhibition of iron-molybdenum cofactor
biosynthesis by L127Delta NifH and NifNE. J. Biol. Chem. 274, 29413-29419

Rangaraj P., Ryle, M. J., Lanzilotta, W. N., Ludden, P. W., and Shah, V. K.
1999. In vitro biosynthesis of iron-molybdenum cofactor and
maturation of the nif-encoded apodinitrogenase. Effect of substitution
for NifH with site-specifically altered forms of NifH. J. Biol. Chem.
274, 19778-19784

Lanzilotta, W. N., Parker, V. P., and Seefeldt, L. C. 1999. Thermodynamics of
Nucleotide Interactions with the Iron Protein. Biochim. Biophys.
Acta.
1429, 411-421

Peters, J. W., Lanzilotta, W. N., Lemon, B. J., and Seefeldt, L. C. 1998. X-ray
crystal structure of the Fe-only hydrogenase (CpI) from Clostridium
pasteurianum to 1.8 angstom resolution. Science 282, 1853-1858

Christiansen, J., Goodwin, P. J., Lanzilotta, W. N., Seefeldt, L. C., and Dean,
D.R. 1998. Catalytic abd Biophysical Properties of a Nitrogenase Apo-MoFe
Protein Produced by a nifB-Deletion Mutant of Azotobacter vinelandii.
Biochemistry 37, 12611-12623

Lanzilotta, W. N., Christiansen, J., Dean, D. R., and Seefeldt, L.C. 1998.
Evidence for Coupled Electron and Proton Transfer in the [8Fe-7S]
Cluster of Nitrogenase. Biochemistry 37, 11376-11384



Lanzilotta, W. N., Parker, V. D., and Seefeldt, L. C. 1998. Electron Transfer in
Nitrogenase Analyzed by Marcus Theory: Evidence for Gating by
MgATP Hydrolysis. Biochemistry 37, 399-407

Lanzilotta, W. N. and Seefeldt, L. C. 1997. Changes in the Midpoint Potentials of
the Nitrogensae Metal Centers as a Result of Iron Protein-Molbdenum
Iron Protein Complex Formation. Biochemistry 36, 12976-12983

Lanzilotta, W. N., Fisher, K., and Seefeldt, L.C. 1997. Evidence for Electron
Transfer-Dependent Formation of a Nitrogenase Iron Protein
Molybdenum Iron Protein Tight Complex: The Role of Aspartate 39.
J. Biol. Chem 272, 4157-4165

Lanzilotta, W. N. and Seefeldt, L. C. 1996. Electron Transfer from the Iron
Protein to the P-Clusters of the Molybdenum-Iron Protein.
Biochemistry 35, 16770-16776

Ryle, M. J., Lanzilotta, W. N., and Seefeldt, L. C. 1996. Elucidating the
Mechanism of Nucleotide-Dependent Changes in the Redox Potential
Of the [4Fe-4S] Cluster in Nitrogenase Iron Protein: The Role of
Phenlalanine 135. Biochemistry 35 , 9424-943

Lanzilotta, W. N., Fisher, K., and Seefeldt, L. C. 1996. Evidence for Electron
Transfer from the Nitrogenase Iron Protein to the Molybdenum-Iron
Protein Without MgATP Hydrolysis: Characterization of a Tight
Protein-Protein Complex. Biochemistry 35, 7188-7196

Ryle, M. J., Lanzilotta, W. N., Seefeldt L. C., Scarrow, R. C., and Jensen, G. M.
1996. Circular Dichroism and X-ray Spectroscopies of Azotobacter
vinelandii Nitrogenase Iron Protein. J. Biol. Chem 271, 1551-
1557

Lanzilotta, W. N., Holz, R. C., and Seefeldt, L. C. 1995. Proton NMR
Investigation of the [4Fe-4S]1+ Cluster Environment of Nitrogenase
Iron Protein from Azotobacter vinelandii : Defining Nucleotide
Induced Conformational Changes. Biochemistry 34, 15646-15653.

Lanzilotta, W. N., Ryle, M. J., Seefeldt, L. C. 1995. Nucleotide Hydrolysis and
Protein Conformational Changes in Azotobacter vinelandii Nitrogenase
Iron Protein: Defining the Function of Aspartate 129. Biochemistry
34, 10713-10723

Ryle, M. J., Lanzilotta, W. N., Mortenson, L. E., Watt, G. D., and Seefeldt, L. C.
1995. Evidence for a Central Role of Lysine 15 of Azotobacter
vinelandii Nitrogenase in Nucleotide Binding and Protein
Conformational Changes. J. Biol. Chem 270, 13112-13117

PUBLICATIONS: Chapters/Reviews

Lanzilotta, W.N., and Seefeldt, L.C. 1995. Nucleotide hydrolysis and protein
conformational changes in Azotobacter vinelandii nitrogenase iron
protein: Defining the function of aspartate 129. In Nitrogen
Fixation: Fundamentals and Applications.
I.A. Tikhonovich,
N.A. Provorov, V.I. Romanov, and W.N. Newton, Eds., Kluwer
Academic Publishers, Boston. p. 157.


Seefeldt, L. C., Ryle, M. J., Chan, J. M. and Lanzilotta, W. N. 1997. Nucleotide
Hydrolysis and Electron Transfer Reactions in Nitrogenase Catalysis. In
Biological Nitrogen Fixation for the 21st Century. C.
Elmerich, A. Kondorosi, W. E. Newton, Eds., Kluwer Academic
Publishers, Boston. p. 39


Lanzilotta, W. N. and Seefeldt, L. C. 1997. Electron transfer reactions in
nitrogenase and the role of MgATP hydrolysis. In Biological
Nitrogen Fixation for the 21st Century.
C. Elmerich, A.
Kondorosi, W. E. Newton, Eds., Kluwer Academic Publishers,
Boston. p. 72

Roberts G.P., Thorsteinsson M.V., Kerby R.L., Lanzilotta W.N., Poulos T. 2001.
CooA: a heme-containing regulatory protein that serves as a specific
sensor of both carbon monoxide and redox state. Prog Nucleic Acid
Res Mol Biol.
67. p. 35-63