Reversible Reactions of Nitric Oxide with a Binuclear Iron(III) Nitrophorin Mimic.

ABSTRACT: Construction of functional synthetic systems that can reversibly bind and transport the most biologically important gaseous molecules, oxygen and nitric oxide (NO), remains a contemporary challenge. Myoglobin and nitrophorin perform these respective tasks employing a protein-embedded heme center where one axial iron site is occupied by a histidine residue and the other is available for small molecule ligation, structural features that are extremely difficult to mimic in protein-free environments. Indeed, the hitherto reported designs rely on sophisticated multistep syntheses for limiting access to one of the two axial coordination sites in small molecules. We have shown previously that binuclear Ga(III) and Al(III) corroles have available axial sites, and now report a redox-active binuclea

SUBMITTER: Sharma VK 

PROVIDER: S-EPMC11410176 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature