ArticleDalton transactions (Cambridge, England : 2003)2014
First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes.
Article in Dalton transactions (Cambridge, England : 2003), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed.
- Spectroscopic definition of ferrous active sites in non-heme iron enzymes.Methods in enzymology · 2024Article
- Protein Flexibility of the α-Ketoglutarate-Dependent Oxygenase Factor-Inhibiting HIF-1: Implications for Substrate Binding, Catalysis, and Regulation.Biochemistry · 2019Article
- OJournal of the American Chemical Society · 2018Article
- Global stability of an α-ketoglutarate-dependent dioxygenase (TauD) and its related complexes.Biochimica et biophysica acta. General subjects · 2017Article
- Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Non-heme Fe(II) enzymes exhibit a general mechanistic strategy where binding all cosubstrates opens a coordination site on the Fe(II) for O2 activation. This study shows that strong-donor ligands, steric interactions with the substrate and second-sphere H-bonding to the facial triad carboxylate allow for five-coordinate site formation in this enzyme superfamily.
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Registered trials
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