J. Erman

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Solvent isotope effects on NMR spectral parameters in high-spin ferric hemoproteins: an indirect probe for distal hydrogen bonding.

M. J. Chatfield, J. Satterlee, G. L. La Mar, 1988, Biochimica et biophysica acta.

The effect of complex formation upon the reduction rates of cytochrome c and cytochrome c peroxidase compound II.

J. Erman, P. Cokic, 1987, Biochimica et biophysica acta.

Proton NMR comparison of noncovalent and covalently cross-linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c.

B. Lou, J. Satterlee, J. Erman, 1992, Biochemistry.

Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide.

J. Kraut, Jimin Wang, M. Miller, 1993, Biochemistry.

The cytochrome C peroxidase oxidation of ferrocytochrome C

J. Satterlee, J. Erman, 1996 .

Yeast cytochrome c peroxidase: mechanistic studies via protein engineering.

J. Erman, L. Vitello, 2002, Biochimica et biophysica acta.

The binding of cytochrome c peroxidase and ferricytochrome c. A spectrophotometric determination of the equilibrium association constant as a function of ionic strength.

J. Erman, L. Vitello, 1980, The Journal of biological chemistry.

Binding of Yeast Cytochrome c to Forty-Four Charge-Reversal Mutants of Yeast Cytochrome c Peroxidase: Isothermal Titration Calorimetry.

J. Erman, T. Jacobson, N. M. Pearl, 2015, Biochemistry.

The oxidation of cytochrome c peroxidase by hydrogen peroxide. Characterization of products.

T. Yonetani, J. Erman, 1975, Biochimica et biophysica acta.

Biogels of cytochrome c : Cytochrome c peroxidase complex studied by electron paramagnetic resonance spectroscopy

K. Chen, J. Erman, C. T. Lin, 1996 .

Cytochrome c peroxidase catalyzed oxidations of substitution inert iron(II) complexes.

W. L. Purcell, J. Erman, 1976, Journal of the American Chemical Society.

Mass instability in isolated recombinant FixL heme domains of Bradyrhizobium japonicum.

R. Jimenez, J. Satterlee, C. Suquet, 2008, Biochemistry.

Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: a fluorescence quenching study on the ionic strength dependence of the interaction.

J. Erman, L. Vitello, 1987, Archives of biochemistry and biophysics.

A covalent complex between horse heart cytochrome c and yeast cytochrome c peroxidase: kinetic properties.

J. Satterlee, J. Erman, S. Moench, 1987, Biochimica et biophysica acta.

Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase.

J. Erman, L. Vitello, R. Dowe, 1984, Archives of biochemistry and biophysics.

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.

J. Satterlee, J. Erman, 1983, The Journal of biological chemistry.

Proton homonuclear correlated spectroscopy as an assignment tool for hyperfine-shifted resonances in medium-sized paramagnetic proteins: cyanide-ligated yeast cytochrome c peroxidase as an example.

J. Satterlee, J. Erman, D. J. Russell, 1991, Biochemistry.

A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength.

J. Erman, S. Loo, 1975, Biochemistry.

Kinetic studies of fluoride binding by cytochrome c peroxidase.

J. Erman, 1974, Biochemistry.

Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase.

J. Erman, 1974, Biochemistry.

Reduction Potential Shifts Due to Active Site and Surface Mutations of Yeast Cytochrome c Peroxidase

J. Erman, Cory M. DiCarlo, L. Vitello, 2007 .

Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme.

P. Daum, J. Erman, C. W. Conroy, 1978, Biochimica et biophysica acta.

Cytochrome P-450 and peroxidase chemistry.

S. Sligar, L. Hager, J. Erman, 1994, Advances in inorganic biochemistry.

Versatile Stopped Flow Temperature Jump Apparatus

G. Hammes, J. Erman, 1966 .

pH dependence of cyanide and imidazole binding to the heme domains of Sinorhizobium meliloti and Bradyrhizobium japonicum FixL.

J. Erman, L. Vitello, A. Bidwai, 2015, Journal of inorganic biochemistry.

Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I.

D. Chinchilla, J. Erman, L. Vitello, 2014, Biochemical and biophysical research communications.

Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.

J. Erman, L. Vitello, A. Bidwai, 2013, Biochimica et biophysica acta.

4-nitroimidazole binding to horse metmyoglobin: evidence for preferential anion binding.

J. Erman, L. Vitello, K. C. Taylor, 2000, Archives of biochemistry and biophysics.

Metmyoglobin/azide: the effect of heme-linked ionizations on the rate of complex formation.

J. Merryweather, J. Erman, J. Lin, 1999, Archives of biochemistry and biophysics.

Metmyoglobin/fluoride: effect of distal histidine protonation on the association and dissociation rate constants.

J. Merryweather, J. Erman, L. Vitello, 1998, Archives of biochemistry and biophysics.

Imidazole binding to horse metmyoglobin: dependence upon pH and ionic strength.

J. Erman, J. Lin, L. Vitello, 1998, Archives of biochemistry and biophysics.

Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase.

J. Kraut, M. Miller, J. Erman, 1992, Biochemistry.

The rate of reaction between cytochrome C peroxidase and hydrogen peroxide is not diffusion limited.

J. Erman, S. Loo, 1977, Biochimica et biophysica acta.

Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes.

G. H. Reed, T. Yonetani, H. Yamamoto, 1972, The Journal of biological chemistry.

Apolar distal pocket mutants of yeast cytochrome c peroxidase: Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants.

C. Ayala, J. Erman, L. Vitello, 2015, Biochimica et biophysica acta.

Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene

C. Ayala, J. Erman, L. Vitello, 2013, BMC Biochemistry.

Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry.

J. Erman, T. Jacobson, A. Wasilewski, 2004, Archives of biochemistry and biophysics.

A kinetic study of the alkaline transitions in cytochrome c peroxidase.

J. Erman, B. K. Dhaliwal, 1985, Biochimica et biophysica acta.

Physicochemical characterization of the alkaline denaturation of cytochrome c peroxidase.

J. Erman, R. Dowe, 1985, Biochimica et biophysica acta.

Proton magnetic resonance studies of cytochrome c peroxidase: pD dependence of the isotropically shifted resonances.

J. Satterlee, J. Erman, 1980, Archives of biochemistry and biophysics.

Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I.

J. Kraut, K. Brown, M. Miller, 1993, Biochemistry.

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.

J. Cannon, J. Erman, 1980, Biochimica et biophysica acta.

Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules.

J. Erman, L. Vitello, Siddhartha. Nakani, 2006, Biochemistry.

Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters.

J. Erman, A. Matthis, Andrea L. Matthis, 1995, Biochemistry.

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.

J. Satterlee, J. Erman, S. Moench, 1987, Biochemistry.

Heme accessibility in the ferricytochrome c-cytochrome c peroxidase complex.

J. Erman, L. Hoth, 1984, Biochimica et biophysica acta.

pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase.

J. Erman, C. W. Conroy, 1978, Biochimica et biophysica acta.

Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Transient state kinetics.

J. Erman, H. Jordi, 1974, Biochemistry.

The effect of phospholipid vesicles on the kinetics of reduction of cytochrome c.

J. Cannon, J. Erman, 1978, Biochemical and biophysical research communications.

Proton NMR Studies of Selected Paramagnetic Heme Proteins

I. Constantinidis, J. Satterlee, S. Alam, 1993 .

Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects.

J. Satterlee, J. Erman, 1991, Biochemistry.

Deuterium isotope effect on the heme-coordinated CO vibration band of ferrous cytochrome c peroxidase-CO

J. Satterlee, J. Erman, 1984 .

Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2':3'-cyclic phosphate.

G. Hammes, J. Erman, 1966, Journal of the American Chemical Society.

Detection of an oxyferryl porphyrin pi-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.

J. Kraut, J. Erman, L. Vitello, 1989, Biochemistry.

Temperature, pH, and Solvent Isotope Effects on Cytochrome c Peroxidase Mutant N82A Studied by Proton NMR

T. Poulos, J. Satterlee, J. Erman, 2000, Journal of protein chemistry.

The effect of the Asn82-->Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy.

T. Poulos, J. Satterlee, S. Alam, 1994, European journal of biochemistry.

Cytochrome c/cytochrome c peroxidase complex: effect of binding-site mutations on the thermodynamics of complex formation.

M. Miller, G. Kresheck, J. Erman, 1997, Biochemistry.

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.

J. Erman, T. Jacobson, N. M. Pearl, 2007, Biochemistry.

Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c

J. Satterlee, J. Erman, Q. Yi, 1993 .

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.

J. Kraut, J. Satterlee, J. Erman, 1990, Biochemistry.

pH-dependent spectral and kinetic properties of cytochrome c peroxidase: comparison of freshly isolated and stored enzyme.

J. Erman, L. Vitello, M. Huang, 1990, Biochemistry.

Reduction of cytochrome c peroxidase compounds I and II by ferrocytochrome c. A stopped-flow kinetic investigation.

J. Erman, F. Summers, 1988, The Journal of biological chemistry.

Oxidation of the His-52 --> Leu mutant of cytochrome c peroxidase by p-nitroperoxybenzoic acid: role of the distal histidine in hydroperoxide activation.

J. Erman, L. Vitello, A. H. Palamakumbura, 1999, Biochemistry.

Proton NMR studies of cytochrome c peroxidase mutant N82A: hyperfine resonance assignments, identification of two interconverting enzyme ofecies, quantitating the rate of interconversion, and determination of equilibrium constants.

T. Poulos, J. Satterlee, S. Alam, 1995, Biochemistry.

Studies on cytochrome c peroxidase. XVII. Stoichiometry and mechanism of the reaction of compound ES with donors.

T. Yonetani, A. Coulson, J. Erman, 1971, The Journal of biological chemistry.

Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength.

J. Erman, L. Vitello, A. Matthis, 1995, Biochemistry.

Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase.

G. Kresheck, J. Erman, L. Vitello, 1995, Biochemistry.

Cytochrome c peroxidase catalyzed oxidation of ferrocytochrome c by hydrogen peroxide: ionic strength dependence of the steady-state rate parameters.

J. Erman, L. Vitello, D. S. Kang, 1990, Biochemistry.

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.

J. Satterlee, J. Erman, S. Moench, 1987, Biochimica et biophysica acta.

Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH.

J. Erman, Cory M. DiCarlo, L. Vitello, 2011, Journal of inorganic biochemistry.

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.

J. Erman, Cory M. DiCarlo, L. Vitello, 2007, Journal of inorganic biochemistry.

Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase.

G. Helms, J. Satterlee, M. Savenkova, 2001, Biochemistry.

Thermometric and Surfactant Selective Potentiometric Titration Studies of Surfactant Binding to Phospholipid Vesicles

G. Kresheck, J. Erman, K. Kale, 1982 .

Calorimetric studies of the thermal denaturation of cytochrome c peroxidase.

G. Kresheck, J. Erman, 1988, Biochemistry.

Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase.

M. Miller, J. Erman, L. Vitello, 1995, Biochemistry.

Proton Nmr Characterization of the Oxidized Forms of Cytochrome c Peroxidase and Soybean Leghemoglobin

J. Satterlee, J. Erman, 1982 .

pH dependence of cyanide binding to the ferric heme domain of the direct oxygen sensor from Escherichia coli and the effect of alkaline denaturation.

J. Erman, A. Bidwai, Esther Y Ok, 2008, Biochemistry.

Active-site mutations in cytochrome c peroxidase : a critical role for histidine-52 in the rate of formation of compound I

J. Kraut, Mark A Miller, J. Erman, 1992 .

Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: properties of CcP mutants H52D, H52E, H52N, and H52Q.

J. Erman, L. Vitello, M. Foshay, 2011, Biochimica et biophysica acta.

Deuterium exchangeable proton hyperfine resonances of low-spin cytochrome c peroxidase and the mechanism of peroxidase catalysis.

J. Satterlee, J. Erman, 1983, Biochimica et biophysica acta.

Polymer-Surfactant Interactions by Surfactant Selective Electrodes

G. Kresheck, J. Erman, K. Kale, 1982 .

Proton Nuclear Magnetic Resonance Studies of Non-Covalent Complexes of Yeast Cytochrome c Peroxidase with Cytochromes c

J. Satterlee, S. Alam, J. Erman, 1993 .

Laue diffraction study on the structure of cytochrome c peroxidase compound I.

V. Fülöp, J. Hajdu, R. P. Phizackerley, 1994, Structure.

Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants.

J. Kraut, J. Erman, L. Vitello, 1990, Biochimica et biophysica acta.

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.

G. Tollin, J. Satterlee, J. Erman, 1988, Biochemistry.

Methionine modification in cytochrome-c peroxidase.

J. Erman, K. Kim, 1988, Biochimica et biophysica acta.

A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound.

T. Yonetani, J. Erman, Takashi Yonetani, 1975, Biochimica et biophysica acta.

Axial histidyl imidazole non-exchangeable proton resonances as indicators of imidazole hydrogen bonding in ferric cyanide complexes of heme peroxidases.

J. Satterlee, G. L. La Mar, J. D. de Ropp, 1982, Biochimica et biophysica acta.

Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L).

D. Chinchilla, J. Erman, L. Vitello, 2015, Biochimica et biophysica acta.

Thermal denaturation of cytochrome c peroxidase: pH dependence.

M. Gross, J. Erman, 1985, Biochimica et biophysica acta.

Cytochrome c peroxidase compound I: formation of covalent protein crosslinks during the endogenous reduction of the active site.

B. Spangler, J. Erman, 1986, Biochimica et biophysica acta.

Assignment of hyperfine shifted resonances in high-spin forms of cytochrome c peroxidase by reconstitutions with deuterated hemins.

J. Satterlee, K. Langry, K. Smith, 1983, Biochimica et biophysica acta.

Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase.

S. Sukits, J. Satterlee, J. Erman, 1997, Biochemistry.

The reaction of hydrogen peroxide with the dimethyl ester heme derivative of cytochrome c peroxidase.

J. Erman, R. Dowe, R. J. Dowe, 1982, The Journal of biological chemistry.

Cytochrome c Peroxidase: A Model Heme Protein

J. Erman, L. Vitello, 1998 .

Electron transfer from cytochrome c to cytochrome c peroxidase across the bilayer lipid membrane (BLM)

Z. Salamon, P. Butko, H. Tien, 1989 .

Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3':5'-cytidine.

G. Hammes, J. Erman, 1966, Journal of the American Chemical Society.

Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly pure holoenzymes.

J. Satterlee, M. Savenkova, J. Erman, 2000, Protein expression and purification.

The effect of ionic strength on the kinetics of fluoride binding to cytochrome c peroxidase.

J. Erman, B. Lent, C. W. Conroy, 1976, Archives of biochemistry and biophysics.

Proton stoichiometry of the cytochrome c peroxidase mechanism as a function of pH.

J. Erman, C. W. Conroy, 1978, Biochimica et biophysica acta.

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.

J. Erman, K. Wilson, T. Jacobson, 2008, Biochemistry.

The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism.

J. Erman, J E Erman, D S Kang, 1982, The Journal of biological chemistry.

pH Dependence of Cyanide Binding to the Ferric Heme Domain of the Direct Oxygen Sensor from Escherichia coli ( Ec DosH) and the Effect of Alkaline Denaturation

J. Erman, A. Bidwai, Esther Y Ok, 2008 .

Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L).

D. Chinchilla, J. Erman, L. Vitello, 2015, Biochimica et biophysica acta.