On the presence of a novel covalently bound oxidation-reduction cofactor, iron and labile sulfur in trimethylamine dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference11 articles.
1. Trimethylamine dehydrogenase from a methylotrophic bacterium I. Isolation and steady-state kinetics
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1. The Interaction of Trimethylamine Dehydrogenase and Electron-transferring Flavoprotein;Journal of Biological Chemistry;2005-05
2. Electron Transfer and Conformational Change in Complexes of Trimethylamine Dehydrogenase and Electron Transferring Flavoprotein;Journal of Biological Chemistry;2002-03
3. Inactivation of C30A Trimethylamine Dehydrogenase by N-Cyclopropyl-α-methylbenzylamine, 1-Phenylcyclopropylamine, and Phenylhydrazine;Biochemistry;2001-06-26
4. Differential Coupling through Val-344 and Tyr-442 of Trimethylamine Dehydrogenase in Electron Transfer Reactions with Ferricenium Ions and Electron Transferring Flavoprotein;Biochemistry;2000-07-11
5. Structural and Biochemical Characterization of Recombinant Wild Type and a C30A Mutant of Trimethylamine Dehydrogenase from Methylophilus methylotrophus (sp. W3A1),;Biochemistry;2000-06-08
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