Article
Assembly of redox centers in the trimethylamine dehydrogenase of bacterium W3A1. Properties of the wild-type enzyme and a C30A mutant expressed from a cloned gene in Escherichia coli.
The Journal of biological chemistry - 13 May 1994
Scrutton N S, Packman L C, Mathews F S, Rohlfs R J, Hille R
Abstract excerpt
In trimethylamine dehydrogenase, the enzyme-bound FMN is covalently linked to Cys-30 by a 6-S-cysteinyl FMN bond. The role played by this bond in catalysis has been investigated using a recombinant wild-type trimethylamine dehydrogenase and a Cys-30 to Ala-30 mutant, both expressed from a cloned...
Topics
- Adenosine Diphosphate
- Bacteria
- Base Sequence
- Chromatography, Gel
- Chromatography, High Pressure Liquid
- Cloning, Molecular
- Electron Spin Resonance Spectroscopy
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Flavin Mononucleotide
- Flavins
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction