Journal
IUBMB LIFE
Volume 62, Issue 10, Pages 776-780Publisher
WILEY
DOI: 10.1002/iub.381
Keywords
human serum heme-albumin; peroxynitrite isomerization; drug binding to Sudlow's site I; kinetics; allosteric inhibition
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Funding
- Ministero dell'Istruzione, dell'Universita e della Ricerca of Italy [PRIN 2007ECX29E_002]
- University Roma Tre, CLAR
- Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, Bari, Italy [I-70126]
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Heme endows human serum albumin (HSA) with globin-like reactivity and spectroscopic properties. Here, the effect of chlorpropamide, digitoxin, furosemide, indomethacin, phenylbutazone, sulfisoxazole, tolbutamide, and warfarin on peroxynitrite isomerization to NO3- by ferric HSA-heme (HSA-heme-Fe(III)) is reported. Drugs binding to Sudlow's site I impair dose-dependently peroxynitrite isomerization by HSA-heme-Fe(III). The allosteric modulation of HSA-heme-Fe(III)-mediated peroxynitrite isomerization by drugs has been ascribed to the pivotal role of Tyr150, a residue that either provides a polar environment in Sudlow's site I or protrudes into the heme cleft (i.e., the fatty acid site 1, FA1), depending on ligand occupancy of either sites. (C) 2010 IUBMB IUBMB Life, 62(10): 776-780, 2010
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