Spin states of and interactions between the hemes of Pseudomonas cyto-chrome c peroxidase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference24 articles.
1. Pseudomonas Cytochrome c Peroxidase. III. The Size and Shape of the Enzyme Molecule.
2. Pseudomonas Cytochrome c Peroxidase. IX. Molecular Weight of the Enzyme in Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis.
3. Electron paramagnetic resonance studies of Pseudomonas cytochrome peroxidase
4. Properties and function of the two hemes in Pseudomonas cytochrome c peroxidase
5. Heme-linked properties of Pseudomonas cytochrome c peroxidase. Evidence for non-equivalence of the hemes
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1. Bacterial peroxidases – Multivalent enzymes that enable the use of hydrogen peroxide for microaerobic and anaerobic proliferation;Coordination Chemistry Reviews;2023-06
2. Cytochrome c peroxidase from Methylococcus capsulatus Bath;Archives of Microbiology;1997-10-15
3. Mössbauer Characterization of Paracoccus denitrificans Cytochrome c Peroxidase;Journal of Biological Chemistry;1995-10
4. Redox and Spin-State Control of the Activity of a Diheme Cytochrome C Peroxidase — Spectroscopic studies;Nuclear Magnetic Resonance of Paramagnetic Macromolecules;1995
5. Nuclear magnetic resonance of paramagnetic metalloproteins;Chemical Reviews;1993-12
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