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Diiron monooxygenases in natural product biosynthesis
Anna J. Komor
, Andrew J. Jasniewski
, Lawrence Que
, John D. Lipscomb
Chemistry (Twin Cities)
Structural Biology and Biophysics (TMED)
Research output
:
Contribution to journal
›
Review article
›
peer-review
43
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Scopus citations
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Keyphrases
Arylamines
100%
Soluble Di-iron Monooxygenase
100%
AurF
100%
Natural Product Biosynthesis
100%
Nitro
66%
Hydroxylation
66%
Aryl
66%
Chloramphenicol
66%
Peroxo Intermediates
66%
Diiron Cluster
66%
Regeneration
33%
Structural Change
33%
Natural Products
33%
Biosynthetic Pathway
33%
Streptomyces
33%
Diiron
33%
Catalytic Conversion
33%
Non-heme
33%
In Situ
33%
O2 Activation
33%
Reaction Pathway
33%
Nonribosomal Peptide Synthetase
33%
Protein Folding
33%
Monooxygenase
33%
Reactive Species
33%
Dinuclear Iron
33%
Iron Clusters
33%
Oxygenation
33%
Metallo-β-lactamase
33%
Oxygenation Reaction
33%
Four-helix Bundle
33%
Streptomyces Venezuelae
33%
Optimization Efficiency
33%
N-oxygenation
33%
Biostatic
33%
Aureothin
33%
Aminobenzoate
33%
Nitrobenzoates
33%
Novel Type
33%
Biochemistry, Genetics and Molecular Biology
Anabolism
100%
Unspecific Monooxygenase
100%
Enzyme
60%
Hydroxylation
40%
Oxygenation
40%
Helix Bundle
20%
Nonribosomal Peptide
20%
Precursor
20%
Streptomyces
20%
Streptomyces Venezuelae
20%
Protein Tertiary Structure
20%