Article
Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.
Protein science : a publication of the Protein Society - 1 Oct 1997
Mulrooney S B, Williams C H
Abstract excerpt
Thioredoxin reductase (TrxR) from Escherichia coli consists of two globular domains connected by a two-stranded beta sheet: an FAD domain and a pyridine nucleotide binding domain. The latter domain contains the redox-active disulfide composed of Cys 135 and Cys 138. TrxR is proposed to undergo a...
Topics
- Adenine Nucleotides
- Amino Acid Sequence
- Binding Sites
- Cysteine
- Disulfides
- Endopeptidases
- Escherichia coli
- Flavin-Adenine Dinucleotide
- Fluorescent Dyes
- Kinetics
- Mutation
- NADP
- Peptide Fragments
- Protein Conformation
- Spectrometry, Fluorescence