Reconstitution of the Fatty Acid Hydroxylase Activity of Cytochrome P450BM-3 Utilizing Its Functional Domains
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium.
2. Coding Nucleotide, 5′ Regulatory, and Deduced Amino Acid Sequences of P-450BM-3, a Single Peptide Cytochrome P-450:NADPH-P-450 Reductase from Bacillus megaterium
3. Characterization of recombinant Bacillus megaterium cytochrome P-450 BM-3 and its two functional domains
4. Expression, purification, and properties of the flavoprotein domain of cytochrome P-450BM-3. Evidence for the importance of the amino-terminal region for FMN binding.
5. Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization
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