Publications
Aconitase
Beinert, H., Kennedy, M.C. and Stout, C.D. (1996) Aconitase as
Iron-Sulfur Protein, Enzyme, and Iron-Regulatory Protein. Chem. Rev. 96:2335-2373.
Lauble, H., Kennedy, M.C., Emptage, M.H., Beinert, H. and Stout, C.D.
(1996) The reaction of fluorocitrate with aconitase and the crystal structure
of the enzyme-inhibitor complex. Proc.
Natl. Acad. Sci. USA 93:13699-13703.
Lloyd.
S.J., Lauble, H., Prasad, G.S. and Stout, C.D. (1999) The
mechanism of aconitase: 1.8 Å resolution crystal structure of the
S642A:citrate complex. Protein Science 8:2655-2662.
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DNA Enzyme
Nowakowski, J., Shim, P.J., Prasad, G.S., Stout, C.D. and Joyce, G.F.
(1999) Crystal structure of an 82-nucleotide RNA-DNA complex formed by the
10-23 DNA enzyme. Nature Struct. Biol. 6:151-156.
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Nowakowski, J., Shim, P.J., Joyce, G.F. and Stout, C.D. (1999)
Combinatorial screening of paired oligonucleotides as an approach to nucleic
acid crystallization. Acta Cryst. D55:1885-1892.
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Nowakowski, J., Shim, P.J., Stout, C.D. and Joyce, G.F. (2000)
Alternative conformations of a nucleic acid four-way junction. J.
Mol. Biol. 300:93-102.
dUTPase
Prasad, G.S.,
Stura, E.A., McRee, D.E., Laco, G.S., Hasselkus-Light, C., Elder, J.H. and
Stout, C.D. (1996) Crystal structure of dUTP Pyrophosphatase from feline
immunodeficiency virus. Protein Science
5:2429-2437.
Prasad,
G.S., Stura, E.A., Elder, J.H. and Stout, C.D. (2000) Crystal
structures of feline immunodeficiency virus dUTP pyrophosphatase and its
nucleotide complexes in three crystal forms.
Acta Cryst. D, in press.
Ferredoxin
Kemper, M.A., Stout, C.D., Lloyd, S.J., Prasad, G.S., Fawcett, S.,
Armstrong, F.A., Shen, B. and Burgess, B.K. (1997) Y13C Azotobacter vinelandii Ferredoxin I:A Designed [Fe-S] Ligand Motif
Contains a Cysteine Persulfide. J. Biol.
Chem. 272:15620-15627.
Sridhar, V., Prasad, G.S., Burgess, B.K. and Stout, C.D. (1998) Crystal
Structures of Ferricyanide Oxidized [Fe-S]
Clusters in Azotobacter vinelandii
Ferredoxin I. J. Biol. Inorg. Chem. 3:140-149.
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Stout, C.D., Stura, E.A. and McRee, D.E. (1998) Structures of Azotobacter
vinelandii 7Fe Ferredoxin at 1.35Å
Resolution and Determination of the [Fe-S] Cluster Bonds with 0.01Å Accuracy.
J.
Mol. Biol. 278:629-639.
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Gao-Sheridan, H.S., Kemper, M.A., Khayat, R., Tilley, G.J., Armstrong,
F.A., Sridhar, V., Prasad, G.S., Stout, C.D. and Burgess, B.K. (1998) A T14C
Variant of Azotobacter vinelandii Ferredoxin
I Undergoes Facile [3Fe-4S]0 to [4Fe-4S]2+ Cluster
Conversion in vitro but not in
vivo. J. Biol. Chem. 273:33692-33701.
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Schipke,
C.G., Goodin, D.B., McRee, D.E. and Stout, C.D. (1999) Oxidized
and Reduced Azotobacter vinelandii Ferredoxin
I at 1.4 Å Resolution: Conformational Change of Surface Residues without
Significant Change in the [3Fe-4S]+/0 Cluster. Biochem. 38:8228-8239.
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Chen, K., Tilley, G.J., Sridhar, V., Prasad, G.S., Stout, C.D.,
Armstrong, F.A. and Burgess, B.K. (1999) Alteration of the Reduction Potential
of the [4Fe-4S]2+/+ Cluster of Azotobacter
vinelandii Ferredoxin I. J. Biol.
Chem. 274:36479-36487.
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Chen, K., Hirst, J., Camba, R., Bonagura, C.A., Stout, C.D., Burgess, B.K.
and Armstrong, F.A. (2000) Atomically defined mechanism for electron-coupled
proton transfer to a buried redox center in a protein. Nature 405:814-817.
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Stout, C. D. (2000) Ferredoxins containing two different Fe-S centers of
the forms [4Fe-4S] and [3Fe-4S]. Handbook
of Metalloproteins (John Wiley and Sons, Ltd.), in press.
Jung, Y.-S., Tilley, G.J., Gao-Sheridan, H.S., Armstrong, F.A., Stout,
C.D. and Burgess, B.K. (2000) Characterization of C42D Azotobacter
vinelandii FdI: A CysXXAspXXCys motif ligates an air stable [4Fe-4S]2+/+
cluster. J. Biol. Chem, submitted.
Ferredoxin Reductase
Prasad, G.S., Kresge, N., Muhlberg, A.B., Shaw, A., Jung, Y.S., Burgess,
B.K. and Stout, C.D. (1998) The Crystal Structure of NADPH: ferredoxin
reductase from Azotoobacter vinelandii.
Protein Science 7:2541-2549.
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Jung, Y.-S., Roberts, V.A., Stout, C.D. and Burgess, B.K. (1999) Complex
Formation between Azotobacter vinelandii
FdI and its Physiological Electron Donor NADPH:Ferredoxin Reductase. J.
Biol. Chem. 274:2978-2987.
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Ribosomal RNP
Agalarov, S.C., Prasad, G.S., Funke, P.M, Stout, C.D. and Williamson, J.R.
(2000) Insights into assembly of the 30S ribosome central domain from the
structure of the S15,S6,S18-rRNA complex. Science 288:107-112.
Sperm Lysin
Vacquier,V.D., Swanson, W.J., Metz, E.C. and Stout, C.D. (1999) Acrosomal
Proteins of Abalone Spermatozoa. Adv.
Develop. Biochem. 5:47-79.
Swanson,
W.J., Metz, E.C., Stout, C.D. and Vacquier, V.D. (1999) Rapid
Evolution of Acrosomal Proteins and Species Specificity of Fertilization in
Abalone. In The Male Gamete: From Basic Science to Clinical Applications, Ed. C.
Gagnon (Cache River Press), Chap. 14, pp. 139-147.
Kresge, N., Vacquier, V.D. and Stout, C.D. (2000) 1.35 and 2.07 Å
resolution structures of the red abalone sperm lysin monomer and dimer reveal
features involved in receptor binding. Acta
Cryst. D56:34-41.
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Kresge, N., Vacquier, V.D. and Stout, C.D. (2000) The high-resolution
crystal structure of green abalone sperm lysin: implications for
species-specific binding of the egg receptor. J.
Mol. Biol. 296:1225-1234.
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Kresge, N., Vacquier, V.D. and Stout, C.D. (2000) Abalone lysin: The
dissolving and evolving sperm protein. Bioessays, submitted.
Transhydrogenase
Prasad, G.S., Sridhar, V., Yamaguchi, M., Hatefi, Y. and Stout, C.D.
(1999) Crystal structure of transhydrogenase domain III at 1.2 Å resolution. Nature
Struct. Biol. 12:1126-1131.
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