In vitro formation of S‐nitrosohemoglobin in red cells by inducible nitric oxide synthase

FEBS Letters

Ferranti, Pasquale²  Mamone, Gianfranco²  Malorni, Antonio²  Sannolo, Nicola¹ 

[1] Istituto di Medicina del Lavoro, II Università, Piazza Miraglia, Naples, Italy;Centro Internazionale di Servizi di Spettrometria di Massa, CNR, via Pansini 5, 80131 Naples, Italy

关键词: Nitric oxide;    Hemoglobin;    S-Nitrosothiol;    S-Nitrosohemoglobin;    Inducible nitric oxide synthase;    Liquid chromatography-electrospray mass spectrometry;    Hb;    hemoglobin;    NO;    nitric oxide;    iNOS;    inducible nitric oxide synthase;    RSNO;    S-nitrosothiol;    HbSNO;    S-nitrosohemoglobin;    metHb;    methemoglobin;    ES/MS;    electrospray mass spectrometry;    LC/ES/MS;    liquid chromatography-electrospray mass spectrometry;    SIM;    single ion monitoring;   

DOI  :  10.1016/S0014-5793(99)01527-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The present study demonstrates that NO produced in vitro by inducible nitric oxide synthase in red cells can convert hemoglobin contained in the red cells to S-nitrosohemoglobin. Experiments carried out either in the absence or in the presence of a low molecular weight thiol, such as cysteine, showed that in the first case the target of NO is heme-Fe²⁺. On the contrary, in the presence of cysteine, the first step is the formation of S-nitrosocysteine, followed by transfer of the NO group to a particular cysteine residue of β-globin, cysteine 93. These results confirm previous data indicating the preferential formation of S-nitrosohemoglobin at that site by chemical methods [Ferranti et al. (1997) FEBS Lett. 400, 17–24], and the existence of a physiological mechanism of inactivation for NO circulating in blood. The analysis of S-nitrosohemoglobin can also allow the quantification of the NO levels in blood to be applied for in vitro and in vivo measurements.

【 授权许可】

Unknown