TAILIEUCHUNG - Báo cáo khoa học: Reductive nitrosylation of ferric human serum heme-albumin

Heme endows human serum albumin (HSA) with heme-protein-like reactiv-ity and spectroscopic properties. Here, the kinetics and thermodynamics of reductive nitrosylation of ferric human serum heme-albumin [HSA-heme-Fe(III)] are reported. All data were obtained at 20 C. At pH , HSA-heme-Fe(III) binds nitrogen monoxide (NO) reversibly, leading to the formation of nitrosylated HSA-heme-Fe(III) [HSA-heme-Fe(III)-NO]. | Reductive nitrosylation of ferric human serum heme-albumin Paolo Ascenzi1 2 Yu Cao1 3 Alessandra di Masi1 Francesca Gullotta1 Giampiero De Sanctis4 Gabriella Fanali5 Mauro Fasano5 and Massimo Coletta3 6 1 Department of Biology University Roma Tre Italy 2 NationalInstitute for Infectious Diseases . Lazzaro Spallanzani Roma Italy 3 Department of ExperimentalMedicine and BiochemicalSciences University of Roma Tor Vergata Italy 4 Department of Molecular Cellular and AnimalBiology University of Camerino Italy 5 Department of Structuraland FunctionalBiology and Center of Neuroscience University of Insubria Busto Arsizio VA Italy 6 Interuniversity Consortium for the Research on the Chemistry of Metals in BiologicalSystems Bari Italy Keywords ferric human serum heme-albumin irreversible reductive nitrosylation kinetics reversible nitrosylation thermodynamics Correspondence P. Ascenzi Department of Biology University Roma Tre Viale Guglielmo Marconi 446 I-00146 Roma Italy Fax 39 06 57336321 Tel 39 06 57333494 E-mail ascenzi@ These authors contributed equally to this study Received 22 December 2009 revised 17 February 2010 accepted 25 March 2010 doi Heme endows human serum albumin HSA with heme-protein-like reactivity and spectroscopic properties. Here the kinetics and thermodynamics of reductive nitrosylation of ferric human serum heme-albumin HSA-heme-Fe III are reported. All data were obtained at 20 C. At pH HSA-heme-Fe III binds nitrogen monoxide NO reversibly leading to the formation of nitrosylated HSA-heme-Fe III HSA-heme-Fe III -NO . By contrast at pH the addition of NO to HSA-heme-Fe III leads to the transient formation of HSA-heme-Fe III -NO in equilibrium with HSA-heme-Fe II -NO . Then HSA-heme-Fe II -NO undergoes nucleophilic attack by OH to yield ferrous human serum heme-albumin HSA-heme-Fe II . HSA-heme-Fe II further reacts with NO to give nitro-sylated HSA-heme-Fe II HSA-heme-Fe II -NO . The .

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