Influence of the Distal His in Imparting Imidazolate Character to the Proximal His in Heme Peroxidase: 1H NMR Study of Cyanide-Inhibited His42Ala Horseradish Peroxidase. De Ropp, J. S., Sham, S., Asokan, A., Newmyer, S., Ortiz de Montellano, P. R., and La Mar, G. N. (2002) J. Am. Chem. Soc. in press
Asp225 and Glu375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase. Colas, C., Kuo, J. M., and Ortiz de Montellano, P. R. (2002) J. Biol. Chem., 277, 7191-7200. HTML, PDF.
Solution 1H NMR of the Molecular and Electronic Structure of the Heme Cavity and Substrate Binding Pocket o High-Spin Ferric Horseradish Peroxidase: Effect of His42Ala Mutation. Asokan, A., de Ropp, J.S., Newmyer, S.L., Ortiz de Montellano, P.R., and La Mar, G.N. (2001) J. Am. Chem. Soc. 123, 4243-4254. HTML, PDF
H2O2-Mediated Cross-Linking between Lactoperoxidase and Myoglobin. Elucidation of Protein -Protein Radical Transfer Reactions. Lardinois, O. M., and Ortiz de Montellano, P. R. (2001) J. Biol. Chem., J. Biol. Chem. 276, 23186-23191. HTML, PDF
EPR Spin-Trapping of a Myeloperoxidase Protein Radical. Lardinois, O.M., and Ortiz de Montellano, P.R. (2000) Biochem. Biophys. Res. Commun. 270, 199-202. Abstra ct, PD F
Spin-Trapping and Protein-Crosslinking of the Lactoperoxidase Protein Radical. Lardinois, O.M., Medzihradszky, K.F., and Ortiz de Montellano, P.R. (1999) J. Biol. Chem. 274, 35441-35448. HTML, PDF
Improvement of Peroxygenase Activity by Reloaction of a Catalytic Histidine within the Active Site of Horseradish Peroxidase. Savenkova, M., Kuo, J. M., and Ortiz de Montellano, P. R. (1998) Biochemistry 37, 10828-10836. HTML PDF
Horseradish Peroxidase: Partial Rescue of the His-42 -> Ala Mutant by a Concurrent Asn-70 -> Asp Mutation. Savenkova, M. I., and Ortiz de Montellano, P. R. (1998) Arch. Biochem. Biophys. 351, 286-293. HTML PDF
Autocatalytic Processing of Heme by Lactoperoxidase Produces the Native Protein-Bound Prosthetic Group. DePillis, G. D., Ozaki, S., Kuo, J. M., Maltby, D. A., and Ortiz de Montellano, P. R. (1997) J. Biol. Chem. 272, 8857-8860. HTML PDF
Rescue of the Horseradish Peroxidase His-170 -> Ala Mutant Activity by Imidazole: Importance of Proximal Ligand Tethering. Newmyer, S. L., Sun, J., Loehr, T. M., and Ortiz de Montellano, P. R. (1996) Biochemistry 35, 12788 - 12795. HTM L
Rescue of His-42 -> Ala Horseradish Peroxidase by a Phe-42 -> His Mutation. Engineering of a Surrogate Catalytic Histidine. Savenkova, M. I., Newmyer, S. L., and Ortiz de Montellano, P. R. (1996) J. Biol. Chem. 271, 24598-24603. HTML PDF
Rescue of the Catalytic Activity of a His-42 -> Ala Mutant of Horseradish Peroxidase by Exogenous Imidazoles. Newmyer, S. L., and Ortiz de Montellano, P. R. (1996) J. Biol. Chem. 271, 14891-14896. HTML PDF
Horseradish Peroxidase His-42->Ala , His-42 -> Val, and Phe-41->Ala Mutants: Histidine Catalysis and Control of Substrate Access to the Heme Iron. Newmyer, S. L., and Ortiz de Montellano, P. R. (1995) J. Biol. Chem. 270, 19430-19438. Abstract HTML
Horseradish Peroxidase Phe-172 -> Tyr Mutant: Sequential Formation of Compound I with a Porphyrin Radical Cation and a Protein Radical. Miller, V. P., Goodin, D. B., Friedman, A., and Ortiz de Montellano, P. R. (1995) J. Biol. Chem. 270, 18413-18419. Abstract HTML
Molecular Engineering of Horseradish Peroxidase: Thioanisole Sulfoxidation and Styrene Epoxidation by Phe-41 Leucine and Threonine Mutants, Ozaki, S., and Ortiz de Montellano, P. R. (1995) J. Am. Chem. Soc. 117, 7056-7064.
Chloroperoxidase-Catalyzed Benzylic Hydroxylation. Miller, V. P., and Ortiz de Montellano, P. R. (1995) Arch. Biochem. Biophys. 319, 333-340.
Molecular Engineering of Horseradish Peroxidase. Highly Enantioselective Sulfoxidation of Aryl Alkyl Sulfides by the F41L Mutant. Ozaki, S., and Ortiz de Montellano, P. R. (1994) J. Am. Chem. Soc. 116, 4487-4488.