Structure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic Biosynthesis

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Structure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic Biosynthesis is …
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scholarly articleQ13442814

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P356DOI10.1021/BI400845B
P3181OpenCitations bibliographic resource ID3024929
P932PMC publication ID3826434
P698PubMed publication ID23980641

P50authorJohn D. LipscombQ38327124
Carrie M WilmotQ42119431
Thomas MakrisQ43152899
P2093author name stringCory J Knoot
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The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a monomodular non-ribosomal peptide synthetase geneQ43751006
Electronic and spectroscopic studies of the non-heme reduced binuclear iron sites of two ribonucleotide reductase variants: comparison to reduced methane monooxygenase and contributions to O2 reactivityQ44810720
Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenasesQ44851116
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Conformational Switches Modulate Protein Interactions in Peptide Antibiotic SynthetasesQ57903771
Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. A novel role for protein-protein interactions in an oxygenase mechanismQ67858553
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Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active siteQ72287448
P433issue38
P407language of work or nameEnglishQ1860
P304page(s)6662-71
P577publication date2013-09-24
P1433published inBiochemistryQ764876
P1476titleStructure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic Biosynthesis
P478volume52

Reverse relations

cites work (P2860)
Q42328466A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase
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