Article
Isolation and characterization of mutated FhlA proteins which activate transcription of the hyc operon (formate hydrogenlyase) of Escherichia coli in the absence of molybdate(1).
FEMS microbiology letters - 1 Mar 2000
Self W T, Shanmugam K T
Abstract excerpt
Escherichia coli growing under anaerobic conditions produces H(2) and CO(2) by the enzymatic cleavage of formate catalyzed by formate hydrogenlyase (FHL) consisting of a molybdoenzyme formate dehydrogenase H (fdhF), hydrogenase 3 (hyc), and intermediate electron carriers (hyc). Transcription of both the fdhF and hyc operons requires the activator, FhlA protein, as well as formate and molybdate. Several fhlA...
Topics
- Bacterial Proteins
- Escherichia coli
- Escherichia coli Proteins
- Formate Dehydrogenases
- Formates
- Hydrogenase
- Lac Operon
- Molybdenum
- Multienzyme Complexes
- Mutation
- Operon
- Recombinant Fusion Proteins
- Sulfurtransferases
- Trans-Activators
- Transcription Factors
- Transcriptional Activation
- beta-Galactosidase