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

Susan J. Moench; Stamatia Chroni; Bih Show Lou; James E. Erman; James D. Satterlee

doi:10.1021/bi00129a015

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

Biochemistry ◽

10.1021/bi00129a015 ◽

1992 ◽

Vol 31 (14) ◽

pp. 3661-3670 ◽

Cited By ~ 32

Author(s):

Susan J. Moench ◽

Stamatia Chroni ◽

Bih Show Lou ◽

James E. Erman ◽

James D. Satterlee

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase

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Ferricytochrome c binding induces detectable proton NMR shift changes in cytochrome c peroxidase-CN

Journal of the American Chemical Society ◽

10.1021/ja00046a044 ◽

1992 ◽

Vol 114 (20) ◽

pp. 7907-7909 ◽

Cited By ~ 6

Author(s):

Qian Yi ◽

James E. Erman ◽

James D. Satterlee

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Ferricytochrome C

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Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c. [Erratum to document cited in CA119:244291]

Biochemistry ◽

10.1021/bi00196a022 ◽

1994 ◽

Vol 33 (30) ◽

pp. 9032-9032

Author(s):

Qian Yi ◽

James E. Erman ◽

James D. Satterlee

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Noncovalent Complexes ◽

Nmr Studies

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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 ◽

10.1021/bi00047a015 ◽

1995 ◽

Vol 34 (47) ◽

pp. 15496-15503 ◽

Cited By ~ 3

Author(s):

Steve L. Alam ◽

James D. Satterlee ◽

J. Matthew Mauro ◽

Thomas L. Poulos ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Equilibrium Constants ◽

Proton Nmr ◽

Resonance Assignments ◽

Cytochrome C Peroxidase ◽

Nmr Studies ◽

Enzyme Species

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The Effect of the Asn82Asp Mutation in Yeast Cytochrome c Peroxidase Studied by Proton NMR Spectroscopy

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1994.tb19997.x ◽

1994 ◽

Vol 224 (1) ◽

pp. 81-87 ◽

Cited By ~ 7

Author(s):

James D. Satterlee ◽

Steve L. Alam ◽

J. Matthew Mauro ◽

James E. Erman ◽

Thomas L. Poulos

Keyword(s):

Nmr Spectroscopy ◽

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Proton Nmr Spectroscopy

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

Electron Transport and Oxygen Utilization ◽

10.1007/978-1-349-06491-5_32 ◽

1982 ◽

pp. 223-227

Author(s):

James E. Erman ◽

James D. Satterlee

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Nmr Characterization ◽

Soybean Leghemoglobin

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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 Enzymology ◽

10.1016/0167-4838(87)90251-2 ◽

1987 ◽

Vol 912 (1) ◽

pp. 87-97 ◽

Cited By ~ 39

Author(s):

James D. Satterlee ◽

Susan J. Moench ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Protein Complexes ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Interacting Protein ◽

Nmr Study ◽

Covalent Complex ◽

Horse Cytochrome

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Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235 .fwdarw. Asn-235 mutant

Biochemistry ◽

10.1021/bi00489a042 ◽

1990 ◽

Vol 29 (37) ◽

pp. 8797-8804 ◽

Cited By ~ 30

Author(s):

James D. Satterlee ◽

James E. Erman ◽

J. Matthew Mauro ◽

Joseph Kraut

Keyword(s):

Escherichia Coli ◽

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Recombinant Enzyme ◽

Nmr Analysis ◽

Wild Type

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

Biochemistry ◽

10.1021/bi00092a007 ◽

1993 ◽

Vol 32 (41) ◽

pp. 10988-10994 ◽

Cited By ~ 18

Author(s):

Qian Yi ◽

James E. Erman ◽

James D. Satterlee

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Noncovalent Complexes ◽

Nmr Studies

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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

Biochemistry ◽

10.1021/bi00232a005 ◽

1991 ◽

Vol 30 (18) ◽

pp. 4398-4405 ◽

Cited By ~ 47

Author(s):

James D. Satterlee ◽

James E. Erman

Keyword(s):

Amino Acids ◽

Cytochrome C ◽

Nmr Assignments ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Two Dimensional ◽

Nuclear Overhauser ◽

Nuclear Overhauser Effects

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Proton NMR and electrophoretic studies of the covalent complex formed by crosslinking yeast cytochrome c peroxidase and horse cytochrome c with water-soluble carbodiimide

Biochemistry ◽

10.1021/bi00387a013 ◽

1987 ◽

Vol 26 (13) ◽

pp. 3821-3826 ◽

Cited By ~ 21

Author(s):

Susan J. Moench ◽

James D. Satterlee ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Proton Nmr ◽

Cytochrome C Peroxidase ◽

Water Soluble ◽

Covalent Complex ◽

Horse Cytochrome

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