ArticleChemical science2016
Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- A new heme enzyme family forms hydrazine groups in diverse biosynthetic pathways.bioRxiv : the preprint server for biology · 2025Article
- The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.Chemical science · 2023Article
- Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification.Journal of the American Chemical Society · 2023Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrophorins (NPs) catalyze the nitrite dismutation reaction that is unprecedented in ferriheme proteins. Despite progress in studying the reaction mechanism, fundamental issues regarding the correlation of the structural features with the nitrite dismutase activity of NPs remain elusive. On the other hand, it has been shown that the nitrite complexes of NPs are unique among those of the ferriheme proteins since some of their electron paramagnetic resonance (EPR) spectra show significant highly anisotropic low spin (HALS) signals with large
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