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[Selectivity of lysozyme oxidation by singlet oxygen]
Biokhimiia (Moscow, Russia)
|July 1, 1976
Summary
Singlet oxygen oxidation destroys tryptophan-62 in lysozyme's active site. Substrate (chitin) protects this crucial residue, preventing oxidation and highlighting residue accessibility in chemical reactions.
Area of Science:
- Biochemistry
- Enzymology
- Protein Chemistry
Context:
- Lysozyme is a key enzyme in the innate immune system.
- Oxidative damage can alter enzyme function and structure.
- Singlet oxygen is a reactive oxygen species implicated in cellular damage.
Purpose:
- To investigate the effect of singlet oxygen oxidation on lysozyme structure and function.
- To identify specific residues susceptible to oxidation.
- To explore the role of substrate binding in protecting the enzyme from oxidative damage.
Summary:
- Peptide analysis of oxidized lysozyme revealed the destruction of tryptophan-62 (Trp-62) at the active site.
- The presence of the substrate, chitin, significantly protected Trp-62 from oxidation.
- This suggests that the accessibility of tryptophan residues influences their susceptibility to singlet oxygen.
Impact:
- Provides insights into the mechanism of enzyme inactivation by reactive oxygen species.
- Highlights the importance of active site integrity for enzyme function.
- Informs strategies for protecting enzymes from oxidative stress in biological and industrial settings.