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Steady-state kinetic analysis of halogenase-supporting flavin reductases BorF and AbeF reveals different kinetic mechanisms.
De Silva, Aravinda J; Sehgal, Rippa; Kim, Jennifer; Bellizzi, John J.
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  • De Silva AJ; Department of Chemistry and Biochemistry, College of Natural Sciences and Mathematics, The University of Toledo Toledo, OH, 43606, USA.
  • Sehgal R; Department of Chemistry and Biochemistry, College of Natural Sciences and Mathematics, The University of Toledo Toledo, OH, 43606, USA.
  • Kim J; Department of Chemistry and Biochemistry, College of Natural Sciences and Mathematics, The University of Toledo Toledo, OH, 43606, USA.
  • Bellizzi JJ; Department of Chemistry and Biochemistry, College of Natural Sciences and Mathematics, The University of Toledo Toledo, OH, 43606, USA. Electronic address: john.bellizzi@utoledo.edu.
Arch Biochem Biophys ; 704: 108874, 2021 06 15.
Article in En | MEDLINE | ID: mdl-33862020
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Riboflavin / Escherichia coli Proteins / FMN Reductase / Escherichia coli / Flavin-Adenine Dinucleotide / Flavin Mononucleotide Language: En Journal: Arch Biochem Biophys Year: 2021 Type: Article Affiliation country: United States
Fulltext
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PubMed Links
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Riboflavin / Escherichia coli Proteins / FMN Reductase / Escherichia coli / Flavin-Adenine Dinucleotide / Flavin Mononucleotide Language: En Journal: Arch Biochem Biophys Year: 2021 Type: Article Affiliation country: United States