These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Binding of porphyrin to horseradish peroxidase: effects on structure and function.
    Author: Sil S, Chakraborti AS.
    Journal: Int J Biol Macromol; 2005 Jul; 36(1-2):16-22. PubMed ID: 15907997.
    Abstract:
    Spectrofluorimetric and spectrophotometric studies were done to understand the binding of hematoporphyrin, a photosensitizer to horseradish peroxidase (EC1.11.1.7). The binding affinity constant (K) decreases as the state of aggregation of the porphyrin increases, while the number of binding sites (approximately 1) remains unchanged. The interaction appears to be mostly hydrophobic, entropy-driven and endothermic process. Hematoporphyrin potentiates horseradish peroxidase-catalyzed H2O2-mediated NADH oxidation, probably by porphyrin-influenced removal of superoxide radicals, which are generated in the system. Conformational change of the protein due to its interaction with porphyrin may be associated with potentiation of the catalytic activity of the enzyme.
    [Abstract] [Full Text] [Related] [New Search]