| Year |
Citation |
Score |
| 2015 |
Bidwai AK, Ahrendt AJ, Sullivan JS, Vitello LB, Erman JE. pH dependence of cyanide and imidazole binding to the heme domains of Sinorhizobium meliloti and Bradyrhizobium japonicum FixL. Journal of Inorganic Biochemistry. 153: 88-102. PMID 26499393 DOI: 10.1016/J.Jinorgbio.2015.10.003 |
0.732 |
|
| 2015 |
Erman JE, Vitello LB, Pearl NM, Jacobson T, Francis M, Alberts E, Kou A, Bujarska K. Binding of Yeast Cytochrome c to Forty-Four Charge-Reversal Mutants of Yeast Cytochrome c Peroxidase: Isothermal Titration Calorimetry. Biochemistry. 54: 4845-54. PMID 26212209 DOI: 10.1021/acs.biochem.5b00686 |
0.414 |
|
| 2015 |
Erman JE, Chinchilla D, Studer J, Vitello LB. Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L). Biochimica Et Biophysica Acta. 1854: 869-81. PMID 25907133 DOI: 10.1016/j.bbapap.2015.04.013 |
0.346 |
|
| 2015 |
Bidwai A, Ayala C, Vitello LB, Erman JE. Apolar distal pocket mutants of yeast cytochrome c peroxidase: Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants. Biochimica Et Biophysica Acta. 1854: 919-29. PMID 25900360 DOI: 10.1016/J.Bbapap.2015.04.014 |
0.796 |
|
| 2015 |
Erman JE, Vitello LB, Pearl NM, Jacobson T, Francis M, Alberts E, Kou A, Bujarska K. Binding of Yeast Cytochrome c to Forty-Four Charge-Reversal Mutants of Yeast Cytochrome c Peroxidase: Isothermal Titration Calorimetry Biochemistry. 54: 4845-4854. DOI: 10.1021/acs.biochem.5b00686 |
0.369 |
|
| 2014 |
Chinchilla D, Kilheeney H, Vitello LB, Erman JE. Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I. Biochemical and Biophysical Research Communications. 443: 200-4. PMID 24291498 DOI: 10.1016/j.bbrc.2013.11.084 |
0.402 |
|
| 2013 |
Erman JE, Kilheeney H, Bidwai AK, Ayala CE, Vitello LB. Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene. Bmc Biochemistry. 14: 19. PMID 23895311 DOI: 10.1186/1471-2091-14-19 |
0.792 |
|
| 2013 |
Bidwai AK, Meyen C, Kilheeney H, Wroblewski D, Vitello LB, Erman JE. Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants. Biochimica Et Biophysica Acta. 1834: 137-48. PMID 23022490 DOI: 10.1016/J.Bbapap.2012.09.005 |
0.82 |
|
| 2011 |
Foshay MC, Vitello LB, Erman JE. Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: properties of CcP mutants H52D, H52E, H52N, and H52Q. Biochimica Et Biophysica Acta. 1814: 525-35. PMID 21354339 DOI: 10.1016/J.Bbapap.2011.02.009 |
0.778 |
|
| 2011 |
DiCarlo CM, Vitello LB, Erman JE. Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH. Journal of Inorganic Biochemistry. 105: 532-7. PMID 21334283 DOI: 10.1016/J.Jinorgbio.2011.01.002 |
0.829 |
|
| 2009 |
Foshay MC, Vitello LB, Erman JE. Relocation of the distal histidine in cytochrome c peroxidase: properties of CcP(W51H), CcP(W51H/H52W), and CcP(W51H/H52L). Biochemistry. 48: 5417-25. PMID 19388664 DOI: 10.1021/Bi9003974 |
0.8 |
|
| 2008 |
Bidwai AK, Ok EY, Erman JE. pH dependence of cyanide binding to the ferric heme domain of the direct oxygen sensor from Escherichia coli and the effect of alkaline denaturation. Biochemistry. 47: 10458-70. PMID 18771281 DOI: 10.1021/Bi800872D |
0.789 |
|
| 2008 |
Pearl NM, Jacobson T, Meyen C, Clementz AG, Ok EY, Choi E, Wilson K, Vitello LB, Erman JE. Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: evidence for a single, catalytically active, cytochrome c binding domain. Biochemistry. 47: 2766-75. PMID 18232645 DOI: 10.1021/bi702271r |
0.479 |
|
| 2008 |
Satterlee JD, Suquet C, Bidwai AK, Erman JE, Schwall L, Jimenez R. Mass instability in isolated recombinant FixL heme domains of Bradyrhizobium japonicum. Biochemistry. 47: 1540-53. PMID 18201102 DOI: 10.1021/Bi701672M |
0.728 |
|
| 2007 |
Pearl NM, Jacobson T, Arisa M, Vitello LB, Erman JE. Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site. Biochemistry. 46: 8263-72. PMID 17580971 DOI: 10.1021/bi700623u |
0.469 |
|
| 2007 |
DiCarlo CM, Vitello LB, Erman JE. Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme. Journal of Inorganic Biochemistry. 101: 603-13. PMID 17275914 DOI: 10.1016/J.Jinorgbio.2006.12.006 |
0.799 |
|
| 2007 |
DiCarlo CM, Vitello LB, Erman JE. Reduction potential shifts due to active site and surface mutations of yeast cytochrome C peroxidase Ecs Transactions. 6: 27-45. DOI: 10.1149/1.2790389 |
0.79 |
|
| 2006 |
Nakani S, Vitello LB, Erman JE. Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules. Biochemistry. 45: 14371-8. PMID 17128976 DOI: 10.1021/Bi061662P |
0.759 |
|
| 2006 |
Nakani S, Viriyakul T, Mitchell R, Vitello LB, Erman JE. Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase. Biochemistry. 45: 9887-93. PMID 16893189 DOI: 10.1021/bi060586n |
0.755 |
|
| 2004 |
Foshay MC, Vitello LB, Erman JE. pH Dependence of heme iron coordination, hydrogen peroxide reactivity, and cyanide binding in cytochrome c peroxidase(H52K). Biochemistry. 43: 5065-72. PMID 15109265 DOI: 10.1021/Bi036240J |
0.821 |
|
| 2004 |
Jacobson T, Williamson J, Wasilewski A, Felesik J, Vitello LB, Erman JE. Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry. Archives of Biochemistry and Biophysics. 422: 125-36. PMID 14759599 DOI: 10.1016/j.abb.2003.12.016 |
0.369 |
|
| 2003 |
Satterlee JD, Savenkova MI, Foshay M, Erman JE. Temperature, pH, and solvent isotope dependent properties of the active sites of resting-state and cyanide-ligated recombinant cytochrome c peroxidase (H52L) revealed by proton hyperfine resonance spectra. Biochemistry. 42: 10772-82. PMID 12962502 DOI: 10.1021/Bi034633C |
0.79 |
|
| 2003 |
Bidwai A, Witt M, Foshay M, Vitello LB, Satterlee JD, Erman JE. Cyanide binding to cytochrome c peroxidase (H52L). Biochemistry. 42: 10764-71. PMID 12962501 DOI: 10.1021/Bi034632K |
0.779 |
|
| 2002 |
Erman JE, Vitello LB. Yeast cytochrome c peroxidase: mechanistic studies via protein engineering. Biochimica Et Biophysica Acta. 1597: 193-220. PMID 12044899 DOI: 10.1016/S0167-4838(02)00317-5 |
0.361 |
|
| 2001 |
Savenkova MI, Satterlee JD, Erman JE, Siems WF, Helms GL. Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase Biochemistry. 40: 12123-12131. PMID 11580287 DOI: 10.1021/bi0111000 |
0.34 |
|
| 2000 |
Satterlee JD, Teske JG, Erman JE, Mauro JM, Poulos TL. Temperature, pH, and solvent isotope effects on cytochrome c peroxidase mutant N82A studied by proton NMR Journal of Protein Chemistry. 19: 535-542. PMID 11195979 DOI: 10.1023/A:1026513818176 |
0.393 |
|
| 2000 |
Taylor KC, Vitello LB, Erman JE. 4-Nitroimidazole binding to horse metmyoglobin: Evidence for preferential anion binding Archives of Biochemistry and Biophysics. 382: 284-295. PMID 11068880 DOI: 10.1006/abbi.2000.2039 |
0.411 |
|
| 1999 |
Palamakumbura AH, Vitello LB, Erman JE. Oxidation of the His-52 → Leu mutant of cytochrome c peroxidase by p- nitroperoxybenzoic acid: Role of the distal histidine in hydroperoxide activation Biochemistry. 38: 15653-15658. PMID 10569951 DOI: 10.1021/bi991498o |
0.455 |
|
| 1999 |
Palamakumbura AH, Foshay MC, Vitello LB, Erman JE. Oxidation of cytochrome c peroxidase to compound I by peroxyacids: evidence for rate-limiting diffusion through the protein matrix. Biochemistry. 38: 15647-52. PMID 10569950 DOI: 10.1021/Bi991497W |
0.785 |
|
| 1999 |
Lin J, Merryweather J, Vitello LB, Erman JE. Metmyoglobin/azide: The effect of heme-linked ionizations on the rate of complex formation Archives of Biochemistry and Biophysics. 362: 148-158. PMID 9917339 DOI: 10.1006/abbi.1998.0991 |
0.337 |
|
| 1998 |
Merryweather J, Summers F, Vitello LB, Erman JE. Metmyoglobin/fluoride: Effect of distal histidine protonation on the association and dissociation rate constants Archives of Biochemistry and Biophysics. 358: 359-368. PMID 9784251 DOI: 10.1006/abbi.1998.0872 |
0.352 |
|
| 1998 |
Lin J, Vitello LB, Erman JE. Imidazole binding to horse metmyoglobin: Dependence upon pH and ionic strength Archives of Biochemistry and Biophysics. 352: 214-228. PMID 9587409 DOI: 10.1006/abbi.1998.0619 |
0.393 |
|
| 1998 |
Erman JE, Vitello LB. Cytochrome c peroxidase: A model heme protein Journal of Biochemistry and Molecular Biology. 31: 307-327. |
0.401 |
|
| 1997 |
Sukits SF, Erman JH, Satterlee JD. Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase Biochemistry. 36: 5251-5259. PMID 9136887 DOI: 10.1021/bi970072b |
0.311 |
|
| 1997 |
Erman JE, Kresheck GC, Vitello LB, Miller MA. Cytochrome c/cytochrome c peroxidase complex: Effect of binding-site mutations on the thermodynamics of complex formation Biochemistry. 36: 4054-4060. PMID 9092837 DOI: 10.1021/bi962632x |
0.439 |
|
| 1997 |
Teske JG, Satterlee ID, Erman JE, Vitello LB. Probing the effects of active site mutations on the catalytic decomposition of hydrogen peroxide by cytochrome C peroxidase Faseb Journal. 11. |
0.33 |
|
| 1995 |
Matthis AL, Vitello LB, Erman JE. Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength Biochemistry. 34: 9991-9999. PMID 7632698 DOI: 10.1021/bi00031a022 |
0.361 |
|
| 1995 |
Matthis AL, Erman JE. Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters Biochemistry. 34: 9985-9990. PMID 7632697 DOI: 10.1021/bi00031a021 |
0.422 |
|
| 1995 |
Kresheck GC, Vitello LB, Erman JE. Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase. Biochemistry. 34: 8398-405. PMID 7599130 DOI: 10.1021/bi00026a022 |
0.383 |
|
| 1995 |
Alam SL, Satterlee JD, Mauro JM, Poulos TL, Erman JE. Proton NMR studies of cytochrome c peroxidase mutant N82A: Hyperfine resonance assignments, identification of two interconverting enzyme species, quantitating the rate of interconversion, and determination of equilibrium constants Biochemistry. 34: 15496-15503. PMID 7492551 |
0.406 |
|
| 1994 |
Satterlee JD, Alam SL, Mauro JM, Erman JE, Poulos TL. The effect of the Asn82→Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy European Journal of Biochemistry. 224: 81-87. PMID 8076654 DOI: 10.1111/J.1432-1033.1994.Tb19997.X |
0.383 |
|
| 1994 |
Fülöp V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL. Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure (London, England : 1993). 2: 201-8. PMID 8069633 DOI: 10.1016/S0969-2126(00)00021-6 |
0.404 |
|
| 1994 |
Yi Q, Erman JE, Satterlee JD. Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Biochemistry. 33: 12032-41. PMID 7918422 DOI: 10.1021/bi00206a004 |
0.4 |
|
| 1994 |
Yi Q, Erman JE, Satterlee JD. 1H NMR evaluation of yeast isozyme-1 ferricytochrome c equilibrium exchange dynamics in noncovalent complexes with two forms of yeast cytochrome c peroxidase Journal of the American Chemical Society. 116: 1981-1987. |
0.3 |
|
| 1993 |
Vitello LB, Erman JE, Miller MA, Wang J, Kraut J. Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide. Biochemistry. 32: 9807-18. PMID 8396973 DOI: 10.1021/Bi00088A036 |
0.449 |
|
| 1993 |
Erman JE, Vitello LB, Miller MA, Shaw A, Brown KA, Kraut J. Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry. 32: 9798-806. PMID 8396972 DOI: 10.1021/Bi00088A035 |
0.467 |
|
| 1993 |
Moench SJ, Erman JE, Satterlee JD. Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C International Journal of Biochemistry. 25: 1335-1342. PMID 8224380 DOI: 10.1016/0020-711X(93)90087-U |
0.353 |
|
| 1993 |
Yi Q, Erman JE, Satterlee JD. Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c. Biochemistry. 32: 10988-94. PMID 8218164 DOI: 10.1021/bi00092a007 |
0.358 |
|
| 1992 |
Vitello LB, Erman JE, Miller MA, Mauro JM, Kraut J. Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase. Biochemistry. 31: 11524-35. PMID 1332763 |
0.455 |
|
| 1992 |
Moench SJ, Chroni S, Lou BS, Erman JE, Satterlee JD. Proton NMR comparison of noncovalent and covalently cross-linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c Biochemistry®. 31: 3661-3670. PMID 1314646 |
0.337 |
|
| 1992 |
Yi Q, Erman JE, Satterlee JD. Ferricytochrome c binding induces detectable proton NMR shift changes in cytochrome c peroxidase-CN Journal of the American Chemical Society. 114: 7907-7909. DOI: 10.1021/ja00046a044 |
0.308 |
|
| 1990 |
Kim KL, Kang DS, Vitello LB, Erman JE. Cytochrome c peroxidase catalyzed oxidation of ferrocytochrome c by hydrogen peroxide: ionic strength dependence of the steady-state rate parameters. Biochemistry. 29: 9150-9. PMID 2176845 |
0.422 |
|
| 1990 |
Satterlee JD, Erman JE, Mauro JM, Kraut J. Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235 → Asn-235 mutant Biochemistry. 29: 8797-8804. PMID 2176836 |
0.419 |
|
| 1990 |
Vitello LB, Huang M, Erman JE. pH-dependent spectral and kinetic properties of cytochrome c peroxidase: Comparison of freshly isolated and stored enzyme Biochemistry. 29: 4283-4288. PMID 2161680 |
0.417 |
|
| 1990 |
Vitello LB, Erman JE, Mauro JM, Kraut J. Characterization of the hydrogen peroxide - enzyme reaction for two cytochrome c peroxidase mutants Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1038: 90-97. PMID 2156573 DOI: 10.1016/0167-4838(90)90015-8 |
0.405 |
|
| 1989 |
Erman JE, Vitello LB, Matthew Mauro J, Kraut J. Detection of an oxyferryl porphyrin π-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I Biochemistry. 28: 7992-7995. PMID 2557891 |
0.384 |
|
| 1988 |
Summers FE, Erman JE. Reduction of cytochrome c peroxidase compounds I and II by ferrocytochrome c. A stopped-flow kinetic investigation Journal of Biological Chemistry. 263: 14267-14275. PMID 2844764 |
0.339 |
|
| 1988 |
Kresheck GC, Erman JE. Calorimetric studies of the thermal denaturation of cytochrome c peroxidase Biochemistry®. 27: 2490-2496. PMID 2838075 |
0.334 |
|
| 1988 |
Hazzard JT, Moench SJ, Erman JE, Satterlee JD, Tollin G. Kinetics of intracomplex electron transfer and of reduction of the components of covalent and noncovalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinones Biochemistry. 27: 2002-2008. PMID 2837280 |
0.341 |
|
| 1988 |
Kim K, Erman JE. Methionine modification in cytochrome-c peroxidase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 954: 95-107. PMID 2833928 DOI: 10.1016/0167-4838(88)90059-3 |
0.39 |
|
| 1987 |
Cokic P, Erman JE. The effect of complex formation upon the reduction rates of cytochrome c and cytochrome c peroxidase compound II. Biochimica Et Biophysica Acta. 913: 257-71. PMID 3036233 DOI: 10.1016/0167-4838(87)90134-8 |
0.364 |
|
| 1987 |
Satterlee JD, Moench SJ, Erman JE. A proton NMR study of the non-covalent complex of horse cytochrome c and yeast cytochrome-c peroxidase and its comparison with other interacting protein complexes Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 912: 87-97. PMID 3030433 DOI: 10.1016/0167-4838(87)90251-2 |
0.364 |
|
| 1987 |
Erman JE, Kim KL, Vitello LB, Moench SJ, Satterlee JD. A covalent complex between horse heart cytochrome c and yeast cytochrome c peroxidase: kinetic properties Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 1-10. PMID 3024731 DOI: 10.1016/0167-4838(87)90263-9 |
0.417 |
|
| 1987 |
Vitello LB, Erman JE. Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: A fluorescence quenching study on the ionic strength dependence of the interaction Archives of Biochemistry and Biophysics. 258: 621-629. PMID 2823719 DOI: 10.1016/0003-9861(87)90385-7 |
0.392 |
|
| 1987 |
Moench SJ, Satterlee JD, Erman JE. Proton NMR and electrophoretic studies of the covalent complex formed by cross-linking yeast cytochrome c peroxidase and horse cytochrome c with a water-soluble carbodiimide Biochemistry. 26: 3821-3826. PMID 2820477 |
0.337 |
|
| 1986 |
Sprangler BD, Erman JE. Cytochrome c peroxidase compound I: formation of covalent protein crosslinks during the endogenous reduction of the active site Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 872: 155-157. PMID 3015215 DOI: 10.1016/0167-4838(86)90159-7 |
0.372 |
|
| 1985 |
Gross MT, Erman JE. Thermal denaturation of cytochrome c peroxidase: pH dependence Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 830: 140-146. PMID 2990560 DOI: 10.1016/0167-4838(85)90021-4 |
0.359 |
|
| 1985 |
Dowe RJ, Erman JE. Physicochemical characterization of the alkaline denaturation of cytochrome c proxidase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 827: 183-189. PMID 2981558 DOI: 10.1016/0167-4838(85)90088-3 |
0.431 |
|
| 1985 |
Dhaliwal BK, Erman JE. A kinetic study of alkaline transitions in cytochrome c peroxidase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 827: 174-182. PMID 2981557 DOI: 10.1016/0167-4838(85)90087-1 |
0.34 |
|
| 1984 |
Hoth LR, Erman JE. Heme accessibility in the ferricytochrome c-cytochrome c peroxidase complex Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 788: 151-153. PMID 6331511 DOI: 10.1016/0167-4838(84)90308-X |
0.351 |
|
| 1984 |
Dowe RJ, Vitello LB, Erman JE. Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase Archives of Biochemistry and Biophysics. 232: 566-573. PMID 6087732 DOI: 10.1016/0003-9861(84)90574-5 |
0.35 |
|
| 1983 |
Satterlee JD, Erman JE. Deuterium exchangeable proton hyperfine resonances of low-spin cytochrome c peroxidase and the mechanism of peroxidase catalysis Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 743: 149-154. PMID 6297593 DOI: 10.1016/0167-4838(83)90428-4 |
0.315 |
|
| 1983 |
Shelnutt JA, Satterlee JD, Erman JE. Raman difference spectroscopy of heme-linked ionizations in cytochrome c peroxidase Journal of Biological Chemistry. 258: 2168-2173. PMID 6296135 |
0.404 |
|
| 1983 |
Satterlee JD, Erman JE. Temperature and pH dependence of the proton magnetic hyperfine resonances of cytochrome c peroxidase-cyanide. Evidence for hindered vinyl group rotation as a mediator of the enzymes activity Journal of Biological Chemistry. 258: 1050-1056. PMID 6296068 |
0.393 |
|
| 1982 |
Kang DS, Erman JE. The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism. The Journal of Biological Chemistry. 257: 12775-9. PMID 6290481 |
0.382 |
|
| 1982 |
Dowe RJ, Erman JE. The reaction of hydrogen peroxide with the dimethyl ester heme derivative of cytochrome c peroxidase Journal of Biological Chemistry. 257: 2403-2405. PMID 6277897 |
0.435 |
|
| 1981 |
Satterlee JD, Erman JE. Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase Journal of Biological Chemistry. 256: 1091-1093. PMID 6256380 |
0.308 |
|
| 1981 |
Satterlee JD, Erman JE. Heme asymmetry in deuterohemin-reconstituted cytochrome c peroxidase Journal of the American Chemical Society. 103: 199-200. |
0.303 |
|
| 1980 |
Cannon JB, Erman JE. Determination of the equilibrium constant for the binding of ferricytochrome c to phospholipid vesicles and the effect of binding on the reduction rate of cytochrome c Biochimica Et Biophysica Acta. 600: 19-26. PMID 6249360 |
0.374 |
|
| 1980 |
Erman JE, Vitello LB. The binding of cytochrome c peroxidase and ferricytochrome c. A spectrophotometric determination of the equilibrium association constant as a function of ionic strength Journal of Biological Chemistry. 255: 6224-6227. PMID 6248515 |
0.353 |
|
| 1978 |
Cannon JB, Erman JE. The effect of phospholipid vesicles on the kinetics of reduction of cytochrome c Biochemical and Biophysical Research Communications. 84: 254-260. PMID 215140 DOI: 10.1016/0006-291X(78)90290-5 |
0.391 |
|
| 1978 |
Conroy CW, Erman JE. pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase Bba - Protein Structure. 537: 396-405. PMID 31924 DOI: 10.1016/0005-2795(78)90524-X |
0.392 |
|
| 1978 |
Conroy CW, Erman JE. Proton stoichiometry of the cytochrome c peroxidase mechanism as a function of pH Bba - Enzymology. 527: 370-378. PMID 31913 DOI: 10.1016/0005-2744(78)90351-0 |
0.351 |
|
| 1978 |
Conroy CW, Tyma P, Daum PH, Erman JE. Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme Bba - Protein Structure. 537: 62-69. PMID 31188 DOI: 10.1016/0005-2795(78)90602-5 |
0.388 |
|
| 1977 |
Loo S, Erman JE. The rate of reaction between cytochrome C peroxidase and hydrogen peroxide is not diffusion limited Bba - Enzymology. 481: 279-282. PMID 14694 DOI: 10.1016/0005-2744(77)90159-0 |
0.304 |
|
| 1976 |
Purcell WL, Erman JE. Cytochrome c peroxidase catalyzed oxidations of substitution inert iron(II) complexes Journal of the American Chemical Society. 98: 7033-7037. PMID 184138 |
0.344 |
|
| 1976 |
Lent B, Conroy CW, Erman JE. The effect of ionic strength on the kinetics of fluoride binding to cytochrome c peroxidase Archives of Biochemistry and Biophysics. 177: 56-61. PMID 11752 DOI: 10.1016/0003-9861(76)90415-X |
0.432 |
|
| 1975 |
Erman JE. Oxidation of dicyano-bis 1,10 phenanthroline) iron(II) by compounds I and II of cytochrome c peroxidase Bba - Enzymology. 397: 36-42. PMID 238635 DOI: 10.1016/0005-2744(75)90176-X |
0.368 |
|
| 1975 |
Erman JE, Yonetani T. A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound Bba - Protein Structure. 393: 350-357. PMID 238609 DOI: 10.1016/0005-2795(75)90061-6 |
0.381 |
|
| 1975 |
Erman JE, Yonetani T. The oxidation of cytochrome c peroxidase by hydrogen peroxide characterization of products Bba - Protein Structure. 393: 343-349. PMID 238608 DOI: 10.1016/0005-2795(75)90060-4 |
0.325 |
|
| 1975 |
Loo S, Erman JE. A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength Biochemistry. 14: 3467-3470. PMID 238593 |
0.41 |
|
| 1974 |
Jordi HC, Erman JE. Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Transient state kinetics Biochemistry. 13: 3734-3741. PMID 4368558 |
0.368 |
|
| 1974 |
Jordi HC, Erman JE. Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Steady-state kinetics Biochemistry. 13: 3741-3745. PMID 4368557 |
0.397 |
|
| 1974 |
Erman JE. Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase Biochemistry. 13: 39-44. PMID 4357656 |
0.423 |
|
| 1974 |
Erman JE. Kinetic studies of fluoride binding by cytochrome c peroxidase Biochemistry. 13: 34-39. PMID 4357655 |
0.447 |
|
| 1966 |
Erman JE, Hammes GG. Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3′:5′-cytidine Journal of the American Chemical Society. 88: 5614-5617. PMID 5980178 DOI: 10.1021/Ja00975A047 |
0.342 |
|
| 1966 |
Erman JE, Hammes GG. Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2′:3′-cyclic phosphate Journal of the American Chemical Society. 88: 5607-5614. PMID 5980177 DOI: 10.1021/Ja00975A046 |
0.332 |
|
| Show low-probability matches. |