-
1
-
-
0039316844
-
An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata
-
Chen, Y. P., Woodin, S. A., Lincoln, D. E., and Lovell, C. R. (1996) An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata, J. Biol. Chem. 271, 4609-4612.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 4609-4612
-
-
Chen, Y.P.1
Woodin, S.A.2
Lincoln, D.E.3
Lovell, C.R.4
-
2
-
-
0028961335
-
SCOP: A structural classification of proteins database for the investigation of sequences and structures
-
Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 247, 536-540.
-
(1995)
J. Mol. Biol.
, vol.247
, pp. 536-540
-
-
Murzin, A.G.1
Brenner, S.E.2
Hubbard, T.3
Chothia, C.4
-
3
-
-
0034705539
-
The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins
-
LaCount, M. W., Zhang, E. L., Chen, Y. P., Han, K. P., Whitton, M. M., Lincoln, D. E., Woodin, S. A., and Lebioda, L. (2000) The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins, J. Biol. Chem. 275, 18712-18716.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 18712-18716
-
-
Lacount, M.W.1
Zhang, E.L.2
Chen, Y.P.3
Han, K.P.4
Whitton, M.M.5
Lincoln, D.E.6
Woodin, S.A.7
Lebioda, L.8
-
4
-
-
0033619236
-
An enzymatic globin from a marine worm
-
Lebioda, L., LaCount, M. W., Zhang, E., Chen, Y. P., Han, K., Whitton, M. M., Lincoln, D. E., and Woodin, S. A. (1999) An enzymatic globin from a marine worm, Nature 401, 445-445.
-
(1999)
Nature
, vol.401
, pp. 445-445
-
-
Lebioda, L.1
Lacount, M.W.2
Zhang, E.3
Chen, Y.P.4
Han, K.5
Whitton, M.M.6
Lincoln, D.E.7
Woodin, S.A.8
-
5
-
-
0032914442
-
Oxidative 4-dechlorination of 2,4,6-trichlorophenol catalyzed by horseradish peroxidase
-
Ferrari, R. P., Laurenti, E., and Trotta, F. (1999) Oxidative 4-dechlorination of 2,4,6-trichlorophenol catalyzed by horseradish peroxidase, J. Biol. Inorg. Chem. 4, 232-237.
-
(1999)
J. Biol. Inorg. Chem.
, vol.4
, pp. 232-237
-
-
Ferrari, R.P.1
Laurenti, E.2
Trotta, F.3
-
6
-
-
0028907862
-
Spectroscopic investigations on the highly purified lactoperoxidase Fe(III) heme-catalytic site
-
Ferrari, R. P., Laurenti, E., Cecchimi, P. I., Gambino, O., and Sondergaard, I. (1995) Spectroscopic investigations on the highly purified lactoperoxidase Fe(III) heme-catalytic site, J. Inorg. Biochem. 58, 109-127.
-
(1995)
J. Inorg. Biochem.
, vol.58
, pp. 109-127
-
-
Ferrari, R.P.1
Laurenti, E.2
Cecchimi, P.I.3
Gambino, O.4
Sondergaard, I.5
-
8
-
-
0028137199
-
Role of the proximal ligand in peroxidase catalysis - Crystallographic, kinetic, and spectral studies of cytochrome-c peroxidase proximal ligand mutants
-
Choudhury, K., Sundaramoorthy, M., Hickman, A., Yonetani, T., Woehl, E., Dunn, M. F., and Poulos, T. L. (1994) Role of the proximal ligand in peroxidase catalysis - crystallographic, kinetic, and spectral studies of cytochrome-c peroxidase proximal ligand mutants, J. Biol. Chem. 269, 20239-20249.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 20239-20249
-
-
Choudhury, K.1
Sundaramoorthy, M.2
Hickman, A.3
Yonetani, T.4
Woehl, E.5
Dunn, M.F.6
Poulos, T.L.7
-
9
-
-
0027231963
-
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
-
Goodin, D. B., and McRee, D. E. (1993) 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)
Biochemistry
, vol.32
, pp. 3313-3324
-
-
Goodin, D.B.1
McRee, D.E.2
-
10
-
-
0037952979
-
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase
-
Bonagura, C. A., Bhaskar, B., Shimizu, H., Li, H. Y., Sundaramoorthy, M., McRee, D. E., Goodin, D. B., and Poulos, T. L. (2003) High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase, Biochemistry 42, 5600-5608.
-
(2003)
Biochemistry
, vol.42
, pp. 5600-5608
-
-
Bonagura, C.A.1
Bhaskar, B.2
Shimizu, H.3
Li, H.Y.4
Sundaramoorthy, M.5
McRee, D.E.6
Goodin, D.B.7
Poulos, T.L.8
-
11
-
-
0018792074
-
Assignment of the Fe-Nε (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin
-
Kitagawa, T., Nagai, K., and Tsubaki, M. (1979) Assignment of the Fe-Nε (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin, FEBS Lett. 104, 376-378.
-
(1979)
FEBS Lett.
, vol.104
, pp. 376-378
-
-
Kitagawa, T.1
Nagai, K.2
Tsubaki, M.3
-
12
-
-
0011174216
-
Distal and proximal control of ligand reactivity: A transient Raman comparison of COHbA and COHb (Zurich)
-
Scott, T. W., Friedman, J. M., and Macdonald, V. W. (1985) Distal and proximal control of ligand reactivity: A transient Raman comparison of COHbA and COHb (Zurich), J. Am. Chem. Soc. 107, 3702-3705.
-
(1985)
J. Am. Chem. Soc.
, vol.107
, pp. 3702-3705
-
-
Scott, T.W.1
Friedman, J.M.2
Macdonald, V.W.3
-
13
-
-
0032550647
-
The unusual reactivities of Amphirite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazolate proximal heme iron ligand
-
Franzen, S., Roach, M. P., Chen, Y. P., Dyer, R. B., Woodruff, W. H., and Dawson, J. H. (1998) The unusual reactivities of Amphirite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazolate proximal heme iron ligand, J. Am. Chem. Soc. 120, 4658-4661.
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 4658-4661
-
-
Franzen, S.1
Roach, M.P.2
Chen, Y.P.3
Dyer, R.B.4
Woodruff, W.H.5
Dawson, J.H.6
-
14
-
-
0025295712
-
Probing protein structure and dynamics with resonance Raman spectroscopy: Cytochrome c peroxidase and hemoglobin
-
Spiro, T. G., Smulevich, G., and Su, C. (1990) Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin, Biochemistry 29, 4497-4508.
-
(1990)
Biochemistry
, vol.29
, pp. 4497-4508
-
-
Spiro, T.G.1
Smulevich, G.2
Su, C.3
-
15
-
-
0035915343
-
Effect of a charge relay on the vibrational frequencies of carbonmonoxy iron porphine adducts: The coupling of changes in axial ligand bond strength and porphine core size
-
Franzen, S. (2001) Effect of a charge relay on the vibrational frequencies of carbonmonoxy iron porphine adducts: The coupling of changes in axial ligand bond strength and porphine core size, J. Am. Chem. Soc. 123, 12578-12589.
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 12578-12589
-
-
Franzen, S.1
-
17
-
-
0019321508
-
The Stereochemistry of Peroxidase Catalysis
-
Poulos, T. L., and Kraut, J. (1980) The Stereochemistry of Peroxidase Catalysis, J. Biol. Chem. 255, 8199-8205.
-
(1980)
J. Biol. Chem.
, vol.255
, pp. 8199-8205
-
-
Poulos, T.L.1
Kraut, J.2
-
18
-
-
0037173574
-
Mechanisms of compound I formation in heme peroxidases
-
Hiner, A. N. P., Raven, E. L., Thorneley, R. N. F., Garcia-Canovas, F., and Rodriguez-Lopez, J. N. (2002) Mechanisms of compound I formation in heme peroxidases, J. Inorg. Biochem. 91, 27-34.
-
(2002)
J. Inorg. Biochem.
, vol.91
, pp. 27-34
-
-
Hiner, A.N.P.1
Raven, E.L.2
Thorneley, R.N.F.3
Garcia-Canovas, F.4
Rodriguez-Lopez, J.N.5
-
19
-
-
0027514159
-
Crystallographic refinement of lignin peroxidase at 2-Angstrom
-
Poulos, T. L., Edwards, S. L., Wariishi, H., and Gold, M. H. (1993) Crystallographic refinement of lignin peroxidase at 2-Angstrom, J. Biol. Chem. 268, 4429-4440.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 4429-4440
-
-
Poulos, T.L.1
Edwards, S.L.2
Wariishi, H.3
Gold, M.H.4
-
20
-
-
0028913020
-
Identification of a porphyrin pi-cation-radical in ascorbate peroxidase compound-I
-
Patterson, W. R., Poulos, T. L., and Goodin, D. B. (1995) Identification of a porphyrin pi-cation-radical in ascorbate peroxidase compound-I, Biochemistry 34, 4342-4345.
-
(1995)
Biochemistry
, vol.34
, pp. 4342-4345
-
-
Patterson, W.R.1
Poulos, T.L.2
Goodin, D.B.3
-
21
-
-
0028807809
-
A Comparative study of the inactivation of wild-type, recombinant and 2 mutant horseradish-peroxidase isoenzymes-c by hydrogen-peroxide and m-chloroperoxybenzoic acid
-
Hiner, A. N. P., Hernandezruiz, J., Garciacanovas, F., Smith, A. T., Arnao, M. B., and Acosta, M. (1995) A Comparative study of the inactivation of wild-type, recombinant and 2 mutant horseradish-peroxidase isoenzymes-c by hydrogen-peroxide and m-chloroperoxybenzoic acid, Eur. J. Biochem. 234, 506-512.
-
(1995)
Eur. J. Biochem.
, vol.234
, pp. 506-512
-
-
Hiner, A.N.P.1
Hernandezruiz, J.2
Garciacanovas, F.3
Smith, A.T.4
Arnao, M.B.5
Acosta, M.6
-
22
-
-
0023644531
-
Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase
-
Ator, M. A., and Montellano, O. d. (1987) Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase, J. Biol. Chem. 262, 1542-1551.
-
(1987)
J. Biol. Chem.
, vol.262
, pp. 1542-1551
-
-
Ator, M.A.1
Montellano, O.D.2
-
23
-
-
0034794637
-
Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes
-
Han, K., Woodin, S. A., Lincoln, D. E., Fielman, T. E., and Ely, B. (2001) Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes, Mar. Biotechnol. 3, 287-292.
-
(2001)
Mar. Biotechnol.
, vol.3
, pp. 287-292
-
-
Han, K.1
Woodin, S.A.2
Lincoln, D.E.3
Fielman, T.E.4
Ely, B.5
-
24
-
-
14344260370
-
Amphitrite ornata dehaloperoxidase: Enhanced activity for the catalytically active globin using MCPBA
-
Osborne, R. L., Taylor, L. O., Han, K. P., Ely, B., and Dawson, J. H. (2004) Amphitrite ornata dehaloperoxidase: enhanced activity for the catalytically active globin using MCPBA, Biochem. Biophys. Res. Commun. 324, 1194-1198.
-
(2004)
Biochem. Biophys. Res. Commun.
, vol.324
, pp. 1194-1198
-
-
Osborne, R.L.1
Taylor, L.O.2
Han, K.P.3
Ely, B.4
Dawson, J.H.5
-
25
-
-
0027960812
-
Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli
-
Chen, G. F. T., and Inouye, M. (1994) Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli, Genes Dev. 8, 2641-2652.
-
(1994)
Genes Dev.
, vol.8
, pp. 2641-2652
-
-
Chen, G.F.T.1
Inouye, M.2
-
26
-
-
33845488844
-
AGA/AGG codon usage in parasites - Implications for gene expression in Escherichia coli
-
Sayers, J. R., Price, H. P., Fallon, P. G., and Doenhoff, M. J. (1995) AGA/AGG codon usage in parasites - implications for gene expression in Escherichia coli, Parasitol. Today 11, 345-346.
-
(1995)
Parasitol. Today
, vol.11
, pp. 345-346
-
-
Sayers, J.R.1
Price, H.P.2
Fallon, P.G.3
Doenhoff, M.J.4
-
27
-
-
0024284197
-
The AGG codon is translated slowly in Escherichia coli even at very low expression levels
-
Bonekamp, F., and Jensen, K. F. (1988) The AGG codon is translated slowly in Escherichia coli even at very low expression levels, Nucleic Acids Res. 16, 3013-3024.
-
(1988)
Nucleic Acids Res.
, vol.16
, pp. 3013-3024
-
-
Bonekamp, F.1
Jensen, K.F.2
-
30
-
-
28544434326
-
-
MS Thesis in Chemistry, North Carolina State University, Raleigh
-
Chaudhary, C. (2003) MS Thesis in Chemistry, North Carolina State University, Raleigh.
-
(2003)
-
-
Chaudhary, C.1
-
31
-
-
0034605459
-
Imidazole-ligated compound I intermediates: The effects of hydrogen bonding
-
Green, M. T. (2000) Imidazole-ligated compound I intermediates: The effects of hydrogen bonding, J. Am. Chem. Soc. 122, 9495-9499.
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 9495-9499
-
-
Green, M.T.1
-
32
-
-
20444466524
-
Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned?
-
Smulevich, G., Feis, A., and Howes, B. D. (2005) Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned? Acc. Chem. Res. 38, 433-440.
-
(2005)
Acc. Chem. Res.
, vol.38
, pp. 433-440
-
-
Smulevich, G.1
Feis, A.2
Howes, B.D.3
-
33
-
-
0343742523
-
Notomastus lobatus chloroperoxidase and Amphitrite ornata dehaloperoxidase both contain histidine as their proximal heme iron ligand
-
Roach, M. P., Chen, Y. P., Woodin, S. A., Lincoln, D. E., and Dawson, J. H. (1997) Notomastus lobatus chloroperoxidase and Amphitrite ornata dehaloperoxidase both contain histidine as their proximal heme iron ligand, Biochemistry 36, 2197-2202.
-
(1997)
Biochemistry
, vol.36
, pp. 2197-2202
-
-
Roach, M.P.1
Chen, Y.P.2
Woodin, S.A.3
Lincoln, D.E.4
Dawson, J.H.5
-
34
-
-
0037032263
-
An electrostatic model for the frequency shifts in the carbonmonoxy stretching band of myoglobin: Correlation of hydrogen bonding and the Stark tuning rate
-
Franzen, S. (2002) An electrostatic model for the frequency shifts in the carbonmonoxy stretching band of myoglobin: Correlation of hydrogen bonding and the Stark tuning rate, J. Am. Chem. Soc. 124, 13271-13281.
-
(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 13271-13281
-
-
Franzen, S.1
|