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- W1483179972 abstract "Publisher Summary Nitric oxide (NO) is known to bind tightly to the heme iron of hemoglobin (Hb). Innumerable physiological and path physiological roles for NO raised new questions relevant to the functional behavior of Hb. This chapter discusses various schemes for the synthesis of S-nitrosohemoglobin (SNO)-oxyHb, SNO-deoxyHb, and SNO-metHb. The chapter discusses the basic biochemical properties of these molecules and their roles in physiology. S-nitrosodeoxyhemoglobin (SNO-deoxyHb) is synthesized in an anaerobic environment. An equilibrium exsists between nitric oxide (NO) bound to the heme iron of hemoglobin and its reactive cysteine (Cys-/393). The fate of NO and the respiratory cycle are thus intimately related. The chapter also presents a model of the respiratory cycle. The chapter concludes with a discussion of the regulation of local blood flow in vivo by SNO." @default.
- W1483179972 created "2016-06-24" @default.
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- W1483179972 date "1999-01-01" @default.
- W1483179972 modified "2023-10-15" @default.
- W1483179972 title "[11] Concerted nitric oxide/oxygen delivery by hemoglobin" @default.
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- W1483179972 doi "https://doi.org/10.1016/s0076-6879(99)01073-3" @default.
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