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 |
|---|---|
| Pages (from-to) | 1118-1122 |
| Number of pages | 5 |
| Journal | IUBMB Life |
| Volume | 61 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2009 |
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Keywords
- Allosteric modulation
- Heme binding
- Serum heme-albumin
- Serum heme-albumin reactivity
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Clinical Biochemistry
- Molecular Biology
- Genetics
Cite this
Serum heme-albumin : An allosteric protein. / Ascenzi, Paolo; Fasano, Mauro.
In: IUBMB Life, Vol. 61, No. 12, 2009, p. 1118-1122.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Serum heme-albumin
T2 - An allosteric protein
AU - Ascenzi, Paolo
AU - Fasano, Mauro
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
KW - Allosteric modulation
KW - Heme binding
KW - Serum heme-albumin
KW - Serum heme-albumin reactivity
UR - http://www.scopus.com/inward/record.url?scp=77449098529&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77449098529&partnerID=8YFLogxK
U2 - 10.1002/iub.263
DO - 10.1002/iub.263
M3 - Article
C2 - 19946891
AN - SCOPUS:77449098529
VL - 61
SP - 1118
EP - 1122
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 12
ER -