Thermal inactivation of the reductase domain of cytochrome P450 BM3
نویسندگان
چکیده
منابع مشابه
The Flavin-Containing Reductase Domain of Cytochrome P450 BM3 Acts as a Surrogate for Mammalian NADPH-P450 Reductase
Cytochrome P450 BM3 (CYP102A1) from Bacillus megaterium is a self-sufficient monooxygenase that consists of a heme domain and FAD/FMN-containing reductase domain (BMR). In this report, the reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) and 5-cyano-2,3-ditolyl tetrazolium chloride (CTC) by BMR was evaluated as a method for monitoring BMR activity. The electron tr...
متن کاملPhotooxidation of cytochrome P450-BM3.
High-valent iron-oxo species are thought to be intermediates in the catalytic cycles of oxygenases and peroxidases. An attractive route to these iron-oxo intermediates involves laser flash-quench oxidation of ferric hemes, as demonstrated by our work on the ferryl (compound II) and ferryl porphyrin radical cation (compound I) intermediates of horseradish peroxidase. Extension of this work to in...
متن کاملInactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase.
Cytochrome P450 (CYP) monooxygenases catalyze the oxidation of a large number of endogenous compounds and the majority of ingested environmental chemicals, leading to their elimination and often to their metabolic activation to toxic products. This enzyme system therefore provides our primary defense against xenobiotics and is a major determinant in the therapeutic efficacy of pharmacological a...
متن کاملFormation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
Cytochrome P450 BM3 (P450 102) from Bacillus megaterium is a unique bacterial P450, formed from the fusion of a fatty acid hydroxylase to a eukaryotic-like NADPH-cytochrome P450 reductase flavoprotein in a single (1 19 kDa) polypeptide chain (1, 2). It is an attractive model system for enzymological and structural studies due to its homology with mammalian drug metabolising P450 systems, and wi...
متن کاملReduction of dioxygen catalyzed by pyrene-wired heme domain cytochrome P450 BM3 electrodes.
We have electronically wired the cytochrome P450 BM3 heme domain to a graphite electrode with the use of a pyrene-terminated tether. AFM images clearly reveal that pyrene-wired enzyme molecules are adsorbed to the electrode surface. The enzyme-electrode system undergoes rapid and reversible electron transfer, displaying a standard rate constant higher than that of any other P450-electrode syste...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2005
ISSN: 0003-9861
DOI: 10.1016/j.abb.2005.04.022