Article
Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase.
Journal of biochemistry - 1 Nov 1999
Sakamoto K, Mogi T, Noguchi S, Sone N
Abstract excerpt
To probe the location of the quinol oxidation site and physical interactions for inter-subunit electron transfer, we constructed and characterized two chimeric oxidases in which subunit II (CyoA) of cytochrome bo-type ubiquinol oxidase from Escherichia coli was replaced with the counterpart (CaaA) of caa(3)-type cytochrome c oxidase from thermophilic Bacillus PS3. In pHNchi5, the C-terminal hydrophilic domain...
Topics
- Amino Acid Sequence
- Bacillus
- Binding Sites
- Electron Transport
- Electron Transport Complex IV
- Escherichia coli
- Molecular Sequence Data
- Phenotype
- Protein Structure, Tertiary
- Recombinant Fusion Proteins
- Spectrophotometry
- Transformation, Genetic