Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES

M Sivaraja; D. Goodin; M Smith; B. Hoffman

doi:10.1126/science.2549632

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES

Science ◽

10.1126/science.2549632 ◽

1989 ◽

Vol 245 (4919) ◽

pp. 738-740 ◽

Cited By ~ 329

Author(s):

M Sivaraja ◽

D. Goodin ◽

M Smith ◽

B. Hoffman

Keyword(s):

Free Radical ◽

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Radical Site

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Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32631-0 ◽

1983 ◽

Vol 258 (7) ◽

pp. 4356-4363 ◽

Cited By ~ 4

Author(s):

P S Ho ◽

B M Hoffman ◽

C H Kang ◽

E Margoliash

Keyword(s):

Free Radical ◽

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Heme Iron ◽

Radical Site

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Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.76.12.6132 ◽

1979 ◽

Vol 76 (12) ◽

pp. 6132-6136 ◽

Cited By ~ 54

Author(s):

B. M. Hoffman ◽

J. E. Roberts ◽

T. G. Brown ◽

C. H. Kang ◽

E. Margoliash

Keyword(s):

Hydrogen Peroxide ◽

Free Radical ◽

Cytochrome C ◽

Double Resonance ◽

Cytochrome C Peroxidase ◽

Electron Nuclear Double Resonance ◽

Radical Site ◽

Peroxide Compound

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Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical site

Biochemistry ◽

10.1021/bi00125a020 ◽

1992 ◽

Vol 31 (10) ◽

pp. 2789-2797 ◽

Cited By ~ 13

Author(s):

Mark A. Miller ◽

Debkumar Bandyopadhyay ◽

J. Matthew Mauro ◽

Teddy G. Traylor ◽

Joseph Kraut

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Intramolecular Electron Transfer ◽

Compound I ◽

Rapid Reduction ◽

Radical Site

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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 ◽

Cited By ~ 163

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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Binding and oxidation of antithyroid agents in an artificial cavity constructed at the tryptophan radical site of cytochrome C peroxidase

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(95)97538-2 ◽

1995 ◽

Vol 59 (2-3) ◽

pp. 442

Author(s):

Rabi A. Musah ◽

Melissa M. Fitzgerald ◽

Duncan E. McRee ◽

David B. Goodin

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Radical Site ◽

Antithyroid Agents ◽

Artificial Cavity

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Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I

Biochemistry ◽

10.1021/bi00376a004 ◽

1987 ◽

Vol 26 (2) ◽

pp. 351-360 ◽

Cited By ~ 122

Author(s):

Laurence A. Fishel ◽

Jesus E. Villafranca ◽

J. Matthew Mauro ◽

Joseph Kraut

Keyword(s):

Escherichia Coli ◽

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Compound I ◽

Radical Site ◽

Expression In Escherichia Coli

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Structural determinants of the cation binding specificity and ligand pathway to an artificial cavity constructed at the TRP-191 radical site of cytochrome C peroxidase

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(95)97542-x ◽

1995 ◽

Vol 59 (2-3) ◽

pp. 446

Author(s):

Melissa M. Fitzgerald ◽

Gerard M. Jensen ◽

Rabi A. Musah ◽

Michelle L. Trester ◽

Duncan E. McRee ◽

...

Keyword(s):

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Binding Specificity ◽

Cation Binding ◽

Structural Determinants ◽

Radical Site ◽

Artificial Cavity

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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

Biochemistry ◽

10.1021/bi00446a004 ◽

1989 ◽

Vol 28 (20) ◽

pp. 7992-7995 ◽

Cited By ~ 104

Author(s):

James E. Erman ◽

Lidia B. Vitello ◽

J. Matthew Mauro ◽

Joseph Kraut

Keyword(s):

Hydrogen Peroxide ◽

Cytochrome C ◽

Cation Radical ◽

Cytochrome C Peroxidase ◽

Compound I ◽

Radical Intermediate ◽

Radical Site

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Intramolecular electron transfer from the heme to the radical site does not occur in compound II of yeast cytochrome c peroxidase during catalytic turnover

Journal of the American Chemical Society ◽

10.1021/ja00023a059 ◽

1991 ◽

Vol 113 (23) ◽

pp. 8956-8957 ◽

Cited By ~ 17

Author(s):

James T. Hazzard ◽

Gordon Tollin

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Cytochrome C Peroxidase ◽

Intramolecular Electron Transfer ◽

Radical Site ◽

Compound Ii

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Genetically determined conidial longevity is positively correlated with superoxide dismutase, catalase, glutathione peroxidase, cytochrome c peroxidase, and ascorbate free radical reductase activities in Neurospora crassa

Mechanisms of Ageing and Development ◽

10.1016/0047-6374(84)90177-5 ◽

1984 ◽

Vol 24 (1) ◽

pp. 83-100 ◽

Cited By ~ 39

Author(s):

Kenneth D. Munkres ◽

Rajendra S. Rana ◽

Edward Goldstein

Keyword(s):

Superoxide Dismutase ◽

Free Radical ◽

Cytochrome C ◽

Glutathione Peroxidase ◽

Neurospora Crassa ◽

Cytochrome C Peroxidase ◽

Ascorbate Free Radical ◽

Genetically Determined

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