A comparison of the binding properties of myoglobin and cytochrome c shows that the latter, in the reduced state, has an unusually large affinity for ligands, including thioethers. This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1135229 | PMC |
Publication Analysis
Top Keywords
cytochrome iron
8
binding characteristics
4
cytochrome
4
characteristics cytochrome
4
iron comparison
4
comparison binding
4
binding properties
4
properties myoglobin
4
myoglobin cytochrome
4
cytochrome reduced
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!