ArticleJournal of the American Chemical Society2020
A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.
Article in Journal of the American Chemical Society, 2020. 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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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Capturing aBiochemistry · 2023Article
- eMap 2.0: A Web-Based Platform for Identifying electron Transfer Pathways in Proteins and Protein Families.Wiley interdisciplinary reviews. Computational molecular scienceReview
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)═O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here, we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV)═O porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O
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Registered trials
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