TSRI Metallo Program Project Metallo Database

David Goodin Metalloprotein Reprint Request

This form is to submit a request to Dr. Goodin for any of the Metalloprotein publications listed below.


Name and COMPLETE address where reprints should be sent:

 
 
Publications you would like reprints of (check all that apply):

C.G. Schipke, D.B. Goodin, D.E. McRee & C.D. Stout. Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster. Biochemistry, 38, 8228-8239. (1999).

 

S.K. Wilcox, C. Putnam, M. Sastry, J. Blankenship, W.J. Chazin, D.E. McRee & D.B. Goodin. Rational Design of a Functional Metalloenzyme: Introduction of a Site for Manganese Binding and Oxidation into a Heme Peroxidase. submitted to Biochemistry, (1998).

 

G.M. Jensen, S. W. Bunte, A. Warshel & D.B. Goodin. Energetics of Cation Radical formation at the Active Site Tryptophan of Cytochrome-c-Peroxidase and Ascorbate Peroxidase. J. Phys. Chem., in press, (1998).

 

K. Liu, J. Williams, H.-R. Lee, M.M. Fitzgerald, G.M. Jensen, D.B. Goodin & A.E. McDermott. Solid State Deuterium NMR of 2-methylimidazole in CcP (H175G): A Rigid Untethered Imidazole. J. Am. Chem. Soc. in press, (1998).

 

Y. Cao, R.A. Musah, S.K. Wilcox, D.B. Goodin & D.E. McRee. Protein Conformer Selection Observed by Protein Crystallography. Protein Science, 7, 72-78, (1997).

 

R.A. Musah, G.M. Jensen, R.J. Rosenfeld, S.W. Bunte, D.E. McRee & D.B. Goodin. Variation in Strength of a CH to O Hydrogen Bond in an Artificial Cavity. J. Amer, Chem. Soc., 119, 9083-9084, (1997).

 

M.M. Fitzgerald, R.A. Musah, D.E. McRee & D.B. Goodin. A Ligand-Gated, Hinged Loop Rearrangement Opens a Channel to a Buried Artificial Protein Cavity. Nature Struct. Biol. 3, 626-631, (1996).

 

S.K. Wilcox, G.M. Jensen, M.M. Fitzgerald, D.E. McRee & D.B. Goodin. Altering the Substrate Specificity at the Heme Edge of Cytochrome c Peroxidase. Biochemistry 35, 4858-4866, (1996).

 

D.B. Goodin. When an amide is more like histidine than imidazole: the role of axial ligands in heme catalysi. J. Biol. Inorg. Chem. 1, 360-363, (1996).

 

M.M. Fitzgerald, M.L. Trester, G.M. Jensen, D.E. McRee & D.B. Goodin. The Role of Aspartate-235 in the Binding of Cations To an Artificial Cavity at the Radical Site of Cytochrome c Peroxidase. Protein Science 4, 1844-1850, (1995).

 

M.M. Fitzgerald, D.E. McRee, M.J. Churchill & D.B. Goodin. Small Molecule Binding to an Artificially Created Cavity at the Active site of Cytochrome c Peroxidase. Biochemistry 33, 3807-3818, (1994).

 

D.E. McRee, G.M. Jensen, M.M. Fitzgerald, H.A. Siegel & D.B. Goodin. Construction of a Bis-aquo Heme Enzyme and Replacement with Exogenous Ligands. Proc. Natl. Acad. Sci. U.S.A. 91, 12847-12851, (1994).

 

D.B. Goodin & D.E. McRee. The Asp-His-Fe Triad of Cytochrome c Peroxidase Controls the reduction Potential, electronic Structure, and Coupling of the Tryptophan Free-Radical to the Heme. Biochemistry 32, 3313-3324, (1993).


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Last modified: Monday, Oct 11, 1999 at 09:03 (PDT) - Last accessed: Thursday, Aug 17, 2000 at 19:13 (PDT)