scholarly journals Insights into the Role of Substrates on the Interaction between Cytochrome b5 and Cytochrome P450 2B4 by NMR

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Meng Zhang ◽  
Stéphanie V. Le Clair ◽  
Rui Huang ◽  
Shivani Ahuja ◽  
Sang-Choul Im ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome B5 ◽  
Cytochrome P450 2B4

Role of cytochrome b5 in catalysis by cytochrome P450 2B4

2005 ◽  
Vol 338 (1) ◽  
pp. 499-506 ◽  
Author(s):  
Haoming Zhang ◽  
Eugene Myshkin ◽  
Lucy Waskell
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome B5 ◽  
Cytochrome P450 2B4

scholarly journals The role of the length and sequence of the linker domain of cytochrome b5 in stimulating cytochrome P450 2B4 catalysis.

2004 ◽  
Vol 279 (35) ◽  
pp. 36809-36818 ◽  
Author(s):  
Thomas A Clarke ◽  
Sang-Choul Im ◽  
Anil Bidwai ◽  
Lucy Waskell
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome B5 ◽  
Cytochrome P450 2B4 ◽  
Linker Domain

scholarly journals An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation

IUBMB Life ◽  
1997 ◽  
Vol 42 (4) ◽  
pp. 731-737 ◽  
Author(s):  
Yuriy Ivanov ◽  
Irina Kanaeva ◽  
Michail Eldarov ◽  
Konstantin Sklyabin ◽  
Michael Lehnerer ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Complex Formation ◽  
Optical Biosensor ◽  
Interaction Parameters ◽  
Cytochrome P450 2B4

scholarly journals Investigation of the role of cytochrome P450 2B4 active site residues in substrate metabolism based on crystal structures of the ligand-bound enzyme

2006 ◽  
Vol 455 (1) ◽  
pp. 61-67 ◽  
Author(s):  
Cynthia E. Hernandez ◽  
Santosh Kumar ◽  
Hong Liu ◽  
James R. Halpert
Keyword(s):  
Cytochrome P450 ◽  
Crystal Structures ◽  
Active Site ◽  
Active Site Residues ◽  
Substrate Metabolism ◽  
Cytochrome P450 2B4

scholarly journals Substrate-modulated Cytochrome P450 17A1 and Cytochrome b5 Interactions Revealed by NMR

2013 ◽  
Vol 288 (23) ◽  
pp. 17008-17018 ◽  
Author(s):  
D. Fernando Estrada ◽  
Jennifer S. Laurence ◽  
Emily E. Scott
Keyword(s):  
Cytochrome P450 ◽  
Binding Site ◽  
Active Site ◽  
Catalytic Domain ◽  
Cytochrome B5 ◽  
Structural Basis ◽  
Reaction Conditions ◽  
Reversible Binding ◽  
Important Interaction

The membrane heme protein cytochrome b5 (b5) can enhance, inhibit, or have no effect on cytochrome P450 (P450) catalysis, depending on the specific P450, substrate, and reaction conditions, but the structural basis remains unclear. Here the interactions between the soluble domain of microsomal b5 and the catalytic domain of the bifunctional steroidogenic cytochrome P450 17A1 (CYP17A1) were investigated. CYP17A1 performs both steroid hydroxylation, which is unaffected by b5, and an androgen-forming lyase reaction that is facilitated 10-fold by b5. NMR chemical shift mapping of b5 titrations with CYP17A1 indicates that the interaction occurs in an intermediate exchange regime and identifies charged surface residues involved in the protein/protein interface. The role of these residues is confirmed by disruption of the complex upon mutagenesis of either the anionic b5 residues (Glu-48 or Glu-49) or the corresponding cationic CYP17A1 residues (Arg-347, Arg-358, or Arg-449). Cytochrome b5 binding to CYP17A1 is also mutually exclusive with binding of NADPH-cytochrome P450 reductase. To probe the differential effects of b5 on the two CYP17A1-mediated reactions and, thus, communication between the superficial b5 binding site and the buried CYP17A1 active site, CYP17A1/b5 complex formation was characterized with either hydroxylase or lyase substrates bound to CYP17A1. Significantly, the CYP17A1/b5 interaction is stronger when the hydroxylase substrate pregnenolone is present in the CYP17A1 active site than when the lyase substrate 17α-hydroxypregnenolone is in the active site. These findings form the basis for a clearer understanding of this important interaction by directly measuring the reversible binding of the two proteins, providing evidence of communication between the CYP17A1 active site and the superficial proximal b5 binding site.

scholarly journals The stimulatory role of human cytochrome b5 in the bioactivation activities of human CYP1A2, 2A6 and 2E1: a new cell expression system to study cytochrome P450 mediated biotransformation

Mutagenesis ◽  
2005 ◽  
Vol 20 (2) ◽  
pp. 93-100 ◽  
Author(s):  
Maria Paula Duarte ◽  
Bernardo Brito Palma ◽  
Andrei A. Gilep ◽  
António Laires ◽  
José Santos Oliveira ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Expression System ◽  
Cytochrome B5 ◽  
Human Cytochrome ◽  
Cell Expression ◽  
Human Cyp1a2 ◽  
Cell Expression System
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