ArticleACS omega2026
Bottom-Up Model Suggesting Membrane Localization of Heme Oxygenase‑1 Contributes to Heme Selection for Degradation.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
Heme functions as a prosthetic group in numerous hemoproteins, whereas a fraction of intracellular heme is not tightly bound to proteins or membranes and can readily dissociate; this labile heme participates in the regulation of diverse cellular processes. Heme has pro-oxidant properties and is cytotoxic at elevated levels. Accordingly, heme oxygenase-1 (HO-1), an enzyme localized to the endoplasmic reticulum membrane, degrades excess intracellular heme. However, how HO-1 gains access to the excess intracellular heme for degradation remains unclear. In this study, we investigated how the membrane association of HO-1 influences heme capture using a bottom-up approach. A rat HO-1-based fluorescent probe retaining the membrane-anchoring region and capable of detecting heme binding via fluorescence quenching was reconstituted into liposomes composed of 1-palmitoyl-2-oleoyl-
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