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• W1500111907 endingPage "2485" @default.
• W1500111907 startingPage "2474" @default.
• W1500111907 abstract "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 5.5, 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 ≥ 6.5, 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 nitrosylated HSA-heme-Fe(II) [HSA-heme-Fe(II)-NO]. The rate-limiting step for reductive nitrosylation of HSA-heme-Fe(III) is represented by the OH−-mediated reduction of HSA-heme-Fe(II)-NO+ to HSA-heme-Fe(II). The value of the second-order rate constant for OH−-mediated reduction of HSA-heme-Fe(II)-NO+ to HSA-heme-Fe(II) is 4.4 × 103 m−1·s−1. The present results highlight the role of HSA-heme-Fe in scavenging reactive nitrogen species." @default.
• W1500111907 created "2016-06-24" @default.
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• W1500111907 date "2010-04-26" @default.
• W1500111907 modified "2023-10-17" @default.
• W1500111907 title "Reductive nitrosylation of ferric human serum heme-albumin" @default.
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• W1500111907 doi "https://doi.org/10.1111/j.1742-4658.2010.07662.x" @default.
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