Covalent Attachment of an Electroactive Sulphydryl Reagent in Cytochrome P450cam

A University of Oxford study by V. Fulop details the structural and spectroscopic changes in cytochrome P450cam from Pseudomonas putida after modification with an electroactive reagent. The dataset likely contains results from X-ray crystallography at 2.2 Å resolution and electrochemistry experiments. It describes the attachment of two ferrocene molecules, conformational changes in the enzyme's active site, and a shift in the Soret absorption band.

Use Cases

• Modeling protein conformational changes based on structural data from X-ray crystallography.
• Analyzing redox properties of modified enzymes based on described electrochemistry.
• Studying ligand displacement in enzyme active sites based on the replacement of camphor with ferrocene.
• Investigating spectroscopic signatures of heme proteins based on the Soret band shift from 392 to 417 nm.

Strengths

• Structural data is derived from X-ray crystallography at 2.2 Å resolution with an Rcryst of 0.18.
• The description provides specific molecular details, including modification sites at Cys85 and Cys136.

Limitations

• Row count and column-level documentation are absent; field semantics must be inferred after download.
• The dataset is listed as closed license, which restricts reuse and redistribution.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Oxford, author V. Fulop, via paperswithcode.

Collection Method

Experimental data from protein modification, X-ray crystallography, and spectroscopy.