ArticleJournal of the American Chemical Society2025
Unveiling an Ultrareduced State of Heme in Myoglobin.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Synthesis and Optical Properties of Diboron Complexes of 1,4-Anthraquinone Derivatives.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Structural and Electronic Complexities of a Sulfur-Bridged Di-Iron Complex Composed of Mono- and Di-Nitrosyl Units.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
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9 authors.
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Abstract
Heme proteins are essential metalloproteins with diverse biological roles, and these functions are facilitated by the heme's ability to adopt multiple oxidation states, with Fe(II), Fe(III), and Fe(IV) being the most commonly observed. While highly reduced heme states beyond Fe(II) have been studied in synthetic complexes, their presence and characterization in native hemoproteins have remained largely unexplored. In this study, we report a full conversion of sperm whale myoglobin (Mb) to an ultrareduced state through chemical reduction under physiologically relevant conditions. Extensive spectroscopic analyses reveal a concerted proton-coupled two-electron reduction of the porphyrin macrocycle, forming a novel ultrareduced species. The identity of this ultrareduced Mb was determined to be a two-electron reduced product of deoxyMb, Por(2e)Fe(II)-Mb. These experimental data indicate that the reduction reaction is porphyrin ligand-centered, and proton transfer might also be involved, generating a high-spin (
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