Hypoxia (low oxygen level) sensing is a fundamental cellular process contributing to many human diseases. Discoveries of hypoxia and its sensing through the hypoxia-inducible factor (HIF) pathway have provided significant knowledge of cellular responses to low oxygen conditions1. In this study, by applying an interdisciplinary approach, we investigate the reaction of molecular oxygen (O2) and gasotransmitters nitric oxide (NO) and hydrogen sulfide (H2S) with mitoNEET, a [2Fe-2S] iron-sulfur protein located in the mitochondrial outer membrane. Our findings revealed that NO desensitises the mitoNEET [2Fe-2S] clusters towards reduction by H2S. We discovered a specific NO access tunnel to the [2Fe-2S] cluster and found that both O₂ and pioglitazone inhibited NO access to the mitoNEET [2Fe-2S] cluster2. Our findings suggest that the level of molecular O₂ modulates the gasotransmitter sensory action of mitoNEET. These findingshighlight a novel hypoxia-associated mechanism by which mitoNEET influences mitochondrial function and redox signalling (Figure 1), offering new perspectives on its involvement in hypoxia-related diseases such as type-2 diabetes.
Figure 1. A schematic model describing the molecular function of mitoNEET [2Fe-2S] cluster in sensing O2 level and gasotransmitters. Under normoxic conditions, O2 protects the mitoNEET [2Fe-2S] cluster (left). Under inflammatory and hypoxic conditions (right), when the NO level rises, mitoNEET is oxidized by NO and desensitized to H2S reduction (grey). Pioglitazone protects the mitoNEET cluster against NO oxidation and enables H2S reduction (light greeen).