Cytochrome C Peroxidase Mutant Data on Redox and Structural Properties

David B. Goodin of the Scripps Research Institute created this dataset. It contains experimental data on the effects of Asp-235 mutations in cytochrome c peroxidase. The data likely includes measurements of reduction potential, EPR anisotropy, enzyme activity, and zero-field splitting.

Use Cases

• Modeling the relationship between hydrogen bond geometry and reduction potential based on the described 70 mV change.
• Analyzing the effect of the Asp-His-Fe triad on tryptophan free-radical coupling to the heme, as described.
• Predicting enzyme activity and spin-state equilibrium from mutations like D235A, D235N, and D235E.
• Correlating zero-field splitting parameters with redox control mechanisms suggested in the description.

Strengths

• Data is derived from X-ray crystal structure analysis and specific mutations (D235A, D235N, D235E).
• Includes quantitative measurements such as a 70 mV increase in reduction potential for the D235E mutation.
• Examines multiple functional aspects: redox properties, electronic structure, and enzyme activity.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Scripps Research Institute

Collection Method

Likely experimental measurements from X-ray crystallography, EPR spectroscopy, and activity assays.