Structural and enzymological analysis of the interaction of isolated domains of cytochrome P‐450 BM3
- 18 April 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 343 (1), 70-74
- https://doi.org/10.1016/0014-5793(94)80609-8
Abstract
The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain.Keywords
This publication has 26 references indexed in Scilit:
- Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450'sScience, 1993
- Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional proteinBiochemistry, 1991
- Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductaseNature, 1991
- An unusual yet strongly conserved flavoprotein reductase in bacteria and mammalsTrends in Biochemical Sciences, 1991
- An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusionJournal of Molecular Biology, 1990
- The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteinsProtein Engineering, Design and Selection, 1989
- P ‐450 Cytochromes: Structure and FunctionPublished by Wiley ,1987
- Measurement of protein using bicinchoninic acidAnalytical Biochemistry, 1985
- Estimation of globular protein secondary structure from circular dichroismBiochemistry, 1981
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976