Investigation on the interaction between Tetrakis (4-carboxylphenyl) porphyrin and CopC by spectroscopy and docking methods.

CONCLUSION: The results revealed that TCPP can form 1:1 complex with CopC, and the binding constant has been calculated to be (5.88±0.12) × 105 M-1. In addition, it was revealed that TCPP quench the fluorescence of CopC by the static quenching mechanism and the binding site n equals one. The formation of CopC-TCPP complex depended on the hydrophobic force and the distance between TCPP and tryptophan residue in CopC was 2.07 nm. PMID: 31800380 [PubMed - as supplied by publisher]
Source: Protein and Peptide Letters - Category: Biochemistry Authors: Tags: Protein Pept Lett Source Type: research