Search Count: 11
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The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.10 Å Release Date: 1995-07-10 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-07-10
Ligands: HEM
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Crystal Structure Of Yeast Cytochrome C Peroxidase Refined At 1.7-Angstroms Resolution
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:1.70 Å Release Date: 1986-01-21 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM, O |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1986-01-21
Ligands: HEM, O
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Crystallographic Analyses Of Nadh Peroxidase Cys42Ala And Cys42Ser Mutants: Active Site Structure, Mechanistic Implications, And An Unusual Environment Of Arg303
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION Resolution:2.00 Å Release Date: 1995-02-14 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: SO4, FAD |
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION
Release Date: 1995-02-14
Ligands: SO4, FAD
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Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.30 Å Release Date: 1995-07-10 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-07-10
Ligands: HEM
 |
Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:1.90 Å Release Date: 1995-07-10 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-07-10
Ligands: HEM
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Identifying The Physiological Electron Transfer Site Of Cytochrome C Peroxidase By Structure-Based Engineering
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.35 Å Release Date: 1995-12-07 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-12-07
Ligands: HEM
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An L40C Mutation Converts The Cysteine-Sulfenic Acid Redox Centre In Enterococcal Nadh Peroxidase To A Disulfide
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION Resolution:2.00 Å Release Date: 1995-02-14 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: SO4, FAD |
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION
Release Date: 1995-02-14
Ligands: SO4, FAD
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Crystallographic Analyses Of Nadh Peroxidase Cys42Ala And Cys42Ser Mutants: Active Site Structure, Mechanistic Implications, And An Unusual Environment Of Arg303
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION Resolution:2.00 Å Release Date: 1995-02-14 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: SO4, FAD |
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION
Release Date: 1995-02-14
Ligands: SO4, FAD
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The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.10 Å Release Date: 1995-07-10 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: HEM |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-07-10
Ligands: HEM
 |
An L40C Mutation Converts The Cysteine-Sulfenic Acid Redox Centre In Enterococcal Nadh Peroxidase To A Disulfide
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION Resolution:2.10 Å Release Date: 1995-02-14 Classification: OXIDOREDUCTASE (H2O2(A)) Ligands: SO4, FAD |
Organism: Enterococcus faecalis
Method: X-RAY DIFFRACTION
Release Date: 1995-02-14
Ligands: SO4, FAD
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Laue Diffraction Study On The Structure Of Cytochrome C Peroxidase Compound I
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.20 Å Release Date: 2001-07-26 Classification: OXIDOREDUCTASE Ligands: HEM, O |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 2001-07-26
Ligands: HEM, O