Literature DB >> 12078493

Redox properties of vanillyl-alcohol oxidase.

Robert H H van den Heuvel1, Marco W Fraaije, Willem J H van Berkel.   

Abstract

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Year:  2002        PMID： 12078493     DOI： 10.1016/s0076-6879(02)53047-0

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN： 0076-6879            Impact factor:   1.600


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  5 in total

1.  A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate.

Authors:  Jimin Hu; Watchalee Chuenchor; Steven E Rokita
Journal:  J Biol Chem       Date:  2014-11-13       Impact factor: 5.157

2.  Active Site Binding Is Not Sufficient for Reductive Deiodination by Iodotyrosine Deiodinase.

Authors:  Nattha Ingavat; Jennifer M Kavran; Zuodong Sun; Steven E Rokita
Journal:  Biochemistry       Date:  2017-02-16       Impact factor: 3.162

3.  Redox control of iodotyrosine deiodinase.

Authors:  Jimin Hu; Qi Su; Jamie L Schlessman; Steven E Rokita
Journal:  Protein Sci       Date:  2018-10-17       Impact factor: 6.725

4.  Sequence Conservation Does Not Always Signify a Functional Imperative as Observed in the Nitroreductase Superfamily.

Authors:  Jonathan M Musila; Steven E Rokita
Journal:  Biochemistry       Date:  2022-03-23       Impact factor: 3.321

5.  Single Amino Acid Switch between a Flavin-Dependent Dehalogenase and Nitroreductase.

Authors:  Arnab Mukherjee; Steven E Rokita
Journal:  J Am Chem Soc       Date:  2015-12-04       Impact factor: 15.419
  5 in total

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