Cysteine nitrosylation inactivates the HIV-1 protease

Tiziana Persichini, Marco Colasanti, Giuliana M. Lauro, Paolo Ascenzi

Research output: Contribution to journalArticlepeer-review


Nitric oxide (NO) may modulate the catalytic activity of cysteine-containing enzymes. HIV-1 protease action is modulated by the redox equilibrium of Cys67 and Cys95 regulatory residues. In the present study, the inhibitory effect of NO, released by the NO-donor (±)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (NOR-3), on the aspartyl HIV-1 protease action is reported. HIV-1 protease inactivation via NO-mediated nitrosylation of Cys regulatory residue(s) may represent a possible mechanism for inhibition of HIV-1 replication.

Original languageEnglish
Pages (from-to)575-576
Number of pages2
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - Sep 29 1998


  • Cysteine nitrosylation
  • Enzyme inhibition
  • HIV-1 protease
  • Nitric oxide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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