title: Serum heme-albumin: an allosteric protein.
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.
authors: Department of Biology and Interdepartmental Laboratory for Electron Microscopy, University Roma Tre, Viale Guglielmo Marconi 446, Rome, Italy. ascenzi@uniroma3.it
authors: Paolo
authors: P
authors: Ascenzi
authors: Mauro
authors: M
authors: Fasano
mesh_terms: D000418:Albumins / Q000737:chemistry*; D000495:Allosteric Site; D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry; D006418:Heme / Q000737:chemistry*; D006706:Homeostasis; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D008968:Molecular Conformation; D018384:Oxidative Stress; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry
chemical_list: D000418:Albumins; D001798:Blood Proteins; D008024:Ligands; D012709:Serum Albumin; D006418:Heme