Abstract
Heme scavenging by plasma proteins, including serum albumin (SA), provides protection against free-heme oxidative damage, limits access by pathogens to the heme, and contributes to iron homeostasis by recycling the heme iron. In turn, serum heme-albumin (SA-heme) acquires heme-based ligand-binding and (pseudo-)enzymatic properties. Heme binding to SA and SA-heme reactivity are allosterically and competitively modulated by endogenous and exogenous third components, this being relevant in pharmacotherapy management.
Original language | English |
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Pages (from-to) | 1118-1122 |
Number of pages | 5 |
Journal | IUBMB Life |
Volume | 61 |
Issue number | 12 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- Allosteric modulation
- Heme binding
- Serum heme-albumin
- Serum heme-albumin reactivity
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Clinical Biochemistry
- Molecular Biology
- Genetics