Theoretical modeling of the control of reduction potential of heme in cytochrome c peroxidase

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(93)85067-i ◽

1993 ◽

Vol 51 (1-2) ◽

pp. 29

Author(s):

G.M. Jensen ◽

D.E. McRee ◽

D.B. Goodin ◽

A. Warshel

Keyword(s):

Cytochrome C ◽

Reduction Potential ◽

Cytochrome C Peroxidase ◽

Theoretical Modeling

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

Journal of Inorganic Biochemistry ◽

10.1016/j.jinorgbio.2011.01.002 ◽

2011 ◽

Vol 105 (4) ◽

pp. 532-537

Author(s):

Cory M. DiCarlo ◽

Lidia B. Vitello ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Reduction Potential ◽

Cytochrome C Peroxidase

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The Asp-His-iron triad of cytochrome c peroxidase controls the reduction potential electronic structure, and coupling of the tryptophan free radical to the heme

Biochemistry ◽

10.1021/bi00064a014 ◽

1993 ◽

Vol 32 (13) ◽

pp. 3313-3324 ◽

Author(s):

David B. Goodin ◽

Duncan E. McRee

Keyword(s):

Electronic Structure ◽

Free Radical ◽

Cytochrome C ◽

Reduction Potential ◽

Cytochrome C Peroxidase

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

Biochimica et Biophysica Acta (BBA) - Protein Structure ◽

10.1016/0005-2795(78)90602-5 ◽

1978 ◽

Vol 537 (1) ◽

pp. 62-69 ◽

Author(s):

Curtis W. Conroy ◽

Paul Tyma ◽

Peter H. Daum ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Reduction Potential ◽

Cytochrome C Peroxidase ◽

Oxidation Reduction ◽

Oxidation Reduction Potential ◽

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

ECS Transactions ◽

10.1149/1.2790389 ◽

2019 ◽

Vol 6 (6) ◽

pp. 27-45 ◽

Author(s):

Cory M. DiCarlo ◽

Lidia Vitello ◽

James Erman

Keyword(s):

Cytochrome C ◽

Active Site ◽

Reduction Potential ◽

Cytochrome C Peroxidase ◽

Potential Shifts

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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 ◽

10.1016/j.jinorgbio.2006.12.006 ◽

2007 ◽

Vol 101 (4) ◽

pp. 603-613 ◽

Author(s):

Cory M. DiCarlo ◽

Lidia B. Vitello ◽

James E. Erman

Keyword(s):

Cytochrome C ◽

Active Site ◽

Reduction Potential ◽

Cytochrome C Peroxidase ◽

Spectroscopic Properties

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

ECS Meeting Abstracts ◽

10.1149/ma2007-01/8/455 ◽

2007 ◽

Keyword(s):

Cytochrome C ◽

Active Site ◽

Reduction Potential ◽

Cytochrome C Peroxidase ◽

Potential Shifts

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Weak self-association of cytochrome c peroxidase molecules observed by paramagnetic NMR

Journal of Biomolecular NMR ◽

10.1007/s10858-016-0035-z ◽

2016 ◽

Vol 65 (1) ◽

pp. 29-40 ◽

Author(s):

Jesika Schilder ◽

Marcellus Ubbink

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Paramagnetic Nmr ◽

Self Association

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Conversion of the proximal histidine ligand to glutamine restores activity to an inactive mutant of cytochrome c peroxidase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)35655-2 ◽

1992 ◽

Vol 267 (36) ◽

pp. 25656-25659

Author(s):

K Choudhury ◽

M Sundaramoorthy ◽

J.M. Mauro ◽

T.L. Poulos

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase

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Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)33617-2 ◽

1982 ◽

Vol 257 (21) ◽

pp. 13028-13033 ◽

Author(s):

G Daum ◽

P C Böhni ◽

G Schatz

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Intermembrane Space ◽

Yeast Mitochondria

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Oxidation of dicyano-bis 1,10 phenanthroline) iron(II) by compounds I and II of cytochrome c peroxidase

Biochimica et Biophysica Acta (BBA) - Enzymology ◽

10.1016/0005-2744(75)90176-x ◽

1975 ◽

Vol 397 (1) ◽

pp. 36-42 ◽

Author(s):

James E. Erman

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase

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