Serum Heme-Albumin: An Allosteric Protein

被引：72

作者：

Ascenzi, Paolo ^{[1
,2
,3
]}

Fasano, Mauro ^{[4
,5
]}

机构：

[1] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy

[2] Univ Roma Tre, Interdepartmental Lab Electron Microscopy, I-00146 Rome, Italy

[3] Natl Inst Infect Dis IRCCS Lazzaro Spallanzani, Rome, Italy

[4] Univ Insubria, Dept Struct & Funct Biol, Busto Arsizio, VA, Italy

[5] Univ Insubria, Ctr Neurosci, Busto Arsizio, VA, Italy

来源：

IUBMB LIFE | 2009年 / 61卷 / 12期

关键词：

serum heme-albumin; heme binding; serum heme-albumin reactivity; allosteric modulation; SITE-DIRECTED MUTAGENESIS; FATTY-ACID-BINDING; IRON PROTOPORPHYRIN-IX; ANTI-HIV DRUGS; CRYSTAL-STRUCTURE; LIGAND-BINDING; NITRIC-OXIDE; CRYSTALLOGRAPHIC ANALYSIS; ENZYMATIC-PROPERTIES; WARFARIN-BINDING;

D O I：

10.1002/iub.263

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2009 IUBMB IUBMB Life, 61: 1118-1122, 2009

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页码：1118 / 1122

页数：5

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