Reaction of cytochrome c with the radical in cytochrome c peroxidase compound I

1993 ◽  
Vol 115 (8) ◽  
pp. 3372-3373 ◽  
Author(s):  
Seung Hahm ◽  
Lois Geren ◽  
Bill Durham ◽  
Francis Millett
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Compound I

Crystal structure of cytochrome c peroxidase compound I

Biochemistry ◽  
1987 ◽  
Vol 26 (6) ◽  
pp. 1503-1511 ◽  
Author(s):  
Steven L. Edwards ◽  
Nguyen Huu Xuong ◽  
Ronald C. Hamlin ◽  
Joseph Kraut
Keyword(s):  
Crystal Structure ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Compound I

Rate of intramolecular reduction of ferryl iron in compound I of cytochrome c peroxidase

1990 ◽  
Vol 112 (20) ◽  
pp. 7426-7428 ◽  
Author(s):  
Ted Fox ◽  
James T. Hazzard ◽  
Steven L. Edwards ◽  
Ann M. English ◽  
Thomas L. Poulos ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Compound I

Salt-dependent switch in the pathway of electron transfer from cytochrome c to cytochrome c peroxidase compound I

1993 ◽  
Vol 115 (13) ◽  
pp. 5873-5874 ◽  
Author(s):  
Marites R. Nuevo ◽  
Hua Hsien Chu ◽  
Lidia B. Vitello ◽  
James E. Erman
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Compound I

A rapid-scan spectrometric and stopped-flow study of Compound I and Compound II of Pseudomonas cytochrome c peroxidase

1985 ◽  
Vol 236 (2) ◽  
pp. 714-719 ◽  
Author(s):  
Marjaana Rönnberg ◽  
Anne-Marie Lambeir ◽  
Nils Ellfolk ◽  
H.Brian Dunford
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Stopped Flow ◽  
Compound I ◽  
Rapid Scan ◽  
Compound Ii ◽  
Flow Study

Defining substrate specificity and catalytic mechanism in ascorbate peroxidase

2004 ◽  
Vol 71 ◽  
pp. 27-38 ◽  
Author(s):  
Emma L. Raven ◽  
Latesh Lad ◽  
Katherine H. Sharp ◽  
Martin Mewies ◽  
Peter C. E. Moody
Keyword(s):  
Cytochrome C ◽  
Substrate Specificity ◽  
Ascorbate Peroxidase ◽  
Catalytic Mechanism ◽  
Cytochrome C Peroxidase ◽  
Structural Features ◽  
Organic Substrates ◽  
Class Iii ◽  
Compound I ◽  
Functional Features

Haem peroxidases catalyse the H2O2-dependent oxidation of a variety of, usually organic, substrates. Mechanistically, these enzymes are very well characterized: they share a common catalytic cycle that involves formation of a two-electron oxidized intermediate (Compound I) followed by reduction of Compound I by substrate. The substrate specificity is more diverse, however. Most peroxidases oxidize small organic substrates, but there are prominent exceptions to this and the structural features that control substrate specificity remain poorly defined. APX (ascorbate peroxidase) catalyses the H2O2-dependent oxidation of l-ascorbate and has properties that place it at the interface between the class I (e.g. cytochrome c peroxidase) and classical class III (e.g. horseradish peroxidase) peroxidase enzymes. We present a unified analysis of the catalytic and substrate-binding properties of APX, including the crystal structure of the APX-ascorbate complex. Our results provide new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase-mediated catalysis for more than 20 years.

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