The correct dimension on the ordinate of Fig. 1 (panel C) of the main text, and of Fig. 2 of the Supplementary Information is k on instead of k obs .
Drug binding to Sudlow's site I impairs allosterically human serum heme-albumin-catalyzed peroxynitrite detoxification
โ Scribed by Paolo Ascenzi; Alessandro Bolli; Francesca Gullotta; Gabriella Fanali; Mauro Fasano
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 163 KB
- Volume
- 62
- Category
- Article
- ISSN
- 1521-6543
- DOI
- 10.1002/iub.381
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โฆ Synopsis
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 NO 3 -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.
๐ SIMILAR VOLUMES
The authors wish to clarify the following information that was contained in their published article. They regret any confusion caused by the data as originally presented. For graphical reasons, While in the text and in Table 1 values of k on are correctly reported, derivation from slopes in Figure