Correction: The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength
نویسندگان
چکیده
[This corrects the article on p. 755 in vol. 8, PMID: 29163152.].
منابع مشابه
The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength
NADPH-cytochrome P450 reductase (CPR) is a redox partner of microsomal cytochromes P450 and is a prototype of the diflavin reductase family. CPR contains 3 distinct functional domains: a FMN-binding domain (acceptor reduction), a linker (hinge), and a connecting/FAD domain (NADPH oxidation). It has been demonstrated that the mechanism of CPR exhibits an important step in which it switches from ...
متن کاملDistinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.
Multidomain enzymes often rely on large conformational motions to function. However, the conformational setpoints, rates of domain motions and relationships between these parameters and catalytic activity are not well understood. To address this, we determined and compared the conformational setpoints and the rates of conformational switching between closed unreactive and open reactive states i...
متن کاملQuantitative analyses of electrostatic interactions between NADPH-cytochrome P450 reductase and cytochrome P450 enzymes.
A decline in the ionic interactions in the medium with increasing ionic strength (decrease in the ionic activity coefficients) was accompanied by an increase in the fast phase rate constants of CYP2B4 and CYP1A2 reduction. The stimulations were observed both in reconstituted P450 systems and in microsomes. An increase in the ionic strength from 10 to 100 mM sodium phosphate resulted in a 7-fold...
متن کاملPurification and characterization of NADPH-cytochrome P450 reductase from Lake Van fish liver microsomes and investigation of some chemical and metals’ effects on the enzyme activity
NADPH-cytochrome P450 reductase was purified from Lake Van fish liver microsomes by primary and secondary DEAE-cellulose column chromatograph with 20.46 μM/min/mg enzyme specific activities, 54.4% purification yield, and purification of 38-fold. The purity of the enzyme was established, and its monomer molecular weight was determined by SDS-polyacrylamide gel electrophoresis. SDS-PAGE results s...
متن کاملEffect of homomeric P450-P450 complexes on P450 function.
Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this problem, the catalytic activities of several P450s were examined in reconstituted systems containing NADPH-POR (cytochrome P450 reductase) and a si...
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عنوان ژورنال:
دوره 9 شماره
صفحات -
تاریخ انتشار 2018