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Literature DB >> 15900441

The 1.13-A structure of iron-free cytochrome c peroxidase.

Abstract

The iron-free cytochrome c peroxidase (CCP) crystal structure has been determined to 1.13 A and compared with the 1.2-A ferric-CCP structure. Quite unexpectedly, removal of the iron has no effect on porphyrin geometry and distortion, indicating that protein-porphyrin interactions and not iron coordination or formation of the axial His-Fe bond determines porphyrin conformation. However, there are changes in solvent structure in the distal pocket, which lead to changes in the distal His52 acid-base catalyst. The observed ability of His52 to move in response to small changes in solvent structure is very likely important for its role as a catalyst in assisting in the heterolytic fission of the peroxide O-O bond.

Entities: Chemical

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Year: 2005 PMID： 15900441 DOI： 10.1007/s00775-005-0654-4

Source DB: PubMed Journal: J Biol Inorg Chem ISSN： 0949-8257 Impact factor: 3.358

21 in total

1. SHELXL: high-resolution refinement.

Authors: G M Sheldrick; T R Schneider
Journal: Methods Enzymol Date: 1997 Impact factor: 1.600

2. The crystal structure of cytochrome c peroxidase.

Authors: T L Poulos; S T Freer; R A Alden; S L Edwards; U Skogland; K Takio; B Eriksson; N Xuong; T Yonetani; J Kraut
Journal: J Biol Chem Date: 1980-01-25 Impact factor: 5.157

3. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities.

Authors: R M Esnouf
Journal: J Mol Graph Model Date: 1997-04 Impact factor: 2.518

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

Authors: L A Fishel; J E Villafranca; J M Mauro; J Kraut
Journal: Biochemistry Date: 1987-01-27 Impact factor: 3.162

5. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO.

Authors: T A Jones
Journal: Methods Enzymol Date: 1985 Impact factor: 1.600

6. The crystal structure of the iron-free cytochrome c peroxidase and its implication for the enzymatic mechanism.

Authors: X D Su; T Yonetani; U Skoglund
Journal: FEBS Lett Date: 1994-09-12 Impact factor: 4.124

7. The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51.

Authors: D B Goodin; A G Mauk; M Smith
Journal: J Biol Chem Date: 1987-06-05 Impact factor: 5.157

8. Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants.

Authors: K Choudhury; M Sundaramoorthy; A Hickman; T Yonetani; E Woehl; M F Dunn; T L Poulos
Journal: J Biol Chem Date: 1994-08-12 Impact factor: 5.157

4. Subcellular Localization of a Plant Catalase-Phenol Oxidase, AcCATPO, from Amaranthus and Identification of a Non-canonical Peroxisome Targeting Signal.

Authors: Ning Chen; Xiao-Lu Teng; Xing-Guo Xiao
Journal: Front Plant Sci Date: 2017-08-02 Impact factor: 5.753

4 in total

The 1.13-A structure of iron-free cytochrome c peroxidase.

1. SHELXL: high-resolution refinement.

2. The crystal structure of cytochrome c peroxidase.

3. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities.

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

5. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO.

6. The crystal structure of the iron-free cytochrome c peroxidase and its implication for the enzymatic mechanism.

7. The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51.

8. Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants.

9. High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.

10. Compounds I of catalase and horse radish peroxidase: pi-cation radicals.

1. Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.

2. Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase.

Review 3. Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.

4. Subcellular Localization of a Plant Catalase-Phenol Oxidase, AcCATPO, from Amaranthus and Identification of a Non-canonical Peroxisome Targeting Signal.