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 binuclear Fe(III) corrole, (1-Fe)2, in which each (corrolato)Fe(III) center is 5-coordinate, with one axial site occupied by an imidazole from the other corrole. The binuclear structure is further stabilized by attractive forces between the corrole π systems. Reaction of NO with (1-Fe)2 affords mononuclear iron nitrosyls, and of functional relevance, the reaction is reversible: nitric oxide is released upon purging the nitrosyls with inert gases, thereby restoring (1-Fe)2 in solutions or films.
Copyright and License
© 2023 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and re-production in any medium, provided the original work is properly cited.
Acknowledgement
This research was supported by Pazy Foundation (ZG) and A. Mizrahi is appreciated. Research at Caltech was supported by the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health under award number R01DK019038 (HBG). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Additional support for this research at Caltech was provided by the Arnold and Mabel Beckman Foundation. P. H Oyala from Caltech is also appreciated for his help in conducting the EPR experiments.
Data Availability
The data that support the findings of this study are available in the supplementary material of this article.
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Additional details
- ISSN
- 1521-3765
- Pazy Foundation
- 303/19
- National Institutes of Health
- R01DK019038
- Arnold and Mabel Beckman Foundation