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Evidence for Modulation of Oxygen Rebound Rate in Control of Outcome by Iron(II)- And 2-Oxoglutarate-Dependent Oxygenases
Juan Pan
, Eliott S. Wenger
, Megan L. Matthews
, Christopher J. Pollock
, Minakshi Bhardwaj
, Amelia J. Kim
, Benjamin D. Allen
, Robert B. Grossman
,
Carsten Krebs
,
J. Martin Bollinger
Biochemistry & Molecular Biology
Chemistry
Huck Institutes of the Life Sciences
Research output
:
Contribution to journal
›
Article
›
peer-review
38
Scopus citations
Overview
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Keyphrases
Hydroxylated
100%
2-oxoglutarate-dependent Dioxygenase
100%
Oxygen Rebound
100%
Fe(III)
60%
Hydroxylation
40%
Halogenase
40%
Ferryl Intermediate
40%
Halogens
40%
Alternative Outcome
40%
Long-lived
20%
Hydroxide
20%
Deuterium
20%
Bifunctional Enzyme
20%
Aliphatic Carbon
20%
2-oxoglutarate
20%
Norvaline
20%
Carrier Protein
20%
Halogenation
20%
Oxygen Ligands
20%
Oxoferryl
20%
2OG Oxygenases
20%
Oxacycles
20%
Iron-oxo
20%
One-carbon
20%
Biochemistry, Genetics and Molecular Biology
Oxygenase
100%
Rebound
100%
Enzyme
40%
Hydroxylation
40%
Mitochondrial Membrane Transport Protein
20%
Halogenation
20%
Carrier Protein
20%
Neuroscience
Oxytetracycline
50%
Norvaline
50%