Structural and Mutagenesis Studies on the Cytochrome c Peroxidase from Rhodobacter capsulatus Provide New Insights into Structure-Function Relationships of Bacterial Di-heme Peroxidases-Reference-Cited by-同舟云学术

Structural and Mutagenesis Studies on the Cytochrome c Peroxidase from Rhodobacter capsulatus Provide New Insights into Structure-Function Relationships of Bacterial Di-heme Peroxidases

Published:2006-02 Issue:7 Volume:281 Page:4371-4379
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

De Smet Lina,Savvides Savvas N.,Van Horen Ellen,Pettigrew Graham,Van Beeumen Jozef J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. The 44-kDac-type cytochrome induced inRhodobacter capsulatusduring growth with dimethylsulphoxide as an electron acceptor is a cytochromecperoxidase

2. Characterization of cytochrome c-556 from the purple phototrophic bacterium Rhodobacter capsulatus as a cytochrome-c peroxidase

3. A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states.

4. Redox-linked spin-state changes in the di-haem cytochrome c-551 peroxidase from Pseudomonas aeruginosa

5. The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase

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