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Redox biology

NO signal

Nature Chemical Biology volume 19, pages 1178–1179 (2023)Cite this article

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The susceptibility of nitric oxide (NO) to scavenging and oxidation limits its bioavailability and signaling role. New studies indicate that a NO–ferroheme adduct is resistant to such constraints and may serve as an alternative NO-derived signaling molecule in vasculature.

In addition to sGC, many other hemoproteins, such as hemoglobin and myoglobin, also exhibit high affinity for NO and form stable nitrosyl–heme adducts (Fig. 1, process d). However, unlike adducts with sGC, these adducts are short-lived and are oxidized extremely quickly under aerobic conditions. It has been proposed that sGC’s NO-binding rate, which is at least one order of magnitude higher than the binding rate for hemoglobin and myoglobin, offers sufficient advantage to enable NO signaling via diffusible NO in cells with a high sGC/globin ratio2. However, in cells and tissues with abundant competing hemoproteins (i.e., blood, cardiomyocytes or skeletal muscle), intracellular and intravascular diffusion of NO should be severely limited by the hemoproteins' potent NO scavenging, which makes NO signaling difficult. Therefore, alternative NO-derived forms that are resistant to scavenging or oxidative deactivation, such as S-nitrosothiols or other nitrogen oxides, have been suggested to enable NO signaling in these cases.

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Fig. 1: Processes in NO–ferroheme signaling.

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  1. Department of Internal Medicine, The University of Texas Health Science Center at Houston, Houston, TX, USA

    Emil Martin

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  1. Emil Martin
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Correspondence to Emil Martin.

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Martin, E. NO signal. Nat Chem Biol 19, 1178–1179 (2023). https://doi.org/10.1038/s41589-023-01421-3

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