Encontrados 7 documentos, a visualizar página 1 de 1

Ordenado por Data

Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of...

Esteves, Francisco; Almeida, Cristina M.M.; Silva, Sofia; Saldanha, Inês; Urban, Philippe; Rueff, Jose; Pompon, Denis; Truan, Gilles; Kranendonk, Michel

Funding Information: F.E. and M.K.: UID/BIM/0009/2020 of the Portuguese Fundação para a Ciência e a Tecnologia (FCT) and HLTH-2022-STAYHLTH-02/grant agreement 101095679 of the European Horizon´s research and innovation program. Publisher Copyright: © 2023 by the authors.; A unique cytochrome P450 (CYP) oxidoreductase (CPR) sustains activities of human microsomal CYPs. Its function requires toggling between a cl...


The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promi...

Esteves, Francisco; Campelo, Diana; Gomes, Bruno Costa; Urban, Philippe; Bozonnet, Sophie; Lautier, Thomas; Rueff, Jose; Truan, Gilles

NADPH cytochrome P450 oxidoreductase (CPR) is the obligatory electron supplier that sustains the activity of microsomal cytochrome P450 (CYP) enzymes. The variant nature of the isoform-specific proximal interface of microsomal CYPs indicates that CPR is capable of multiple degenerated interactions with CYPs for electron transfer, through different binding mechanisms, and which are still not well-understood. Rec...


Corrigendum

Esteves, Francisco; Campelo, Diana; Gomes, Bruno Costa; Urban, Philippe; Bozonnet, Sophie; Lautier, Thomas; Rueff, Jose; Truan, Gilles

[This corrects the article DOI: 10.3389/fphar.2020.00299.].


Interaction modes of microsomal cytochrome p450s with its reductase and the rol...

Esteves, Francisco; Urban, Philippe; Rueff, Jose; Truan, Gilles; Kranendonk, Michel

The activity of microsomal cytochromes P450 (CYP) is strictly dependent on the supply of electrons provided by NADPH cytochrome P450 oxidoreductase (CPR). The variant nature of the isoform-specific proximal interface of microsomal CYPs implies that the interacting interface between the two proteins is degenerated. Recently, we demonstrated that specific CPR mutations in the FMN-domain (FD) may induce a gain in ...


Probing the role of the hinge segment of cytochrome P450 oxidoreductase in the ...

Campelo, Diana; Esteves, Francisco; Palma, Bernardo Brito; Gomes, Bruno Costa; Rueff, Jose; Lautier, Thomas; Urban, Philippe; Truan, Gilles

NADPH-cytochrome P450 reductase (CPR) is the unique redox partner of microsomal cytochrome P450s (CYPs). CPR exists in a conformational equilibrium between open and closed conformations throughout its electron transfer (ET) function. Previously, we have shown that electrostatic and flexibility properties of the hinge segment of CPR are critical for ET. Three mutants of human CPR were studied (S243P, I245P and R...


Correction

Campelo, Diana; Lautier, Thomas; Urban, Philippe; Esteves, Francisco; Bozonnet, Sophie; Truan, Gilles; Kranendonk, Michel

[This corrects the article on p. 755 in vol. 8, PMID: 29163152.].


The hinge segment of human NADPH-cytochrome P450 reductase in conformational sw...

Campelo, Diana; Lautier, Thomas; Urban, Philippe; Esteves, Francisco; Bozonnet, Sophie; Truan, Gilles; Kranendonk, Michel

This work was in part funded by a joint ANR/FCT program; France: ANR-13-ISV5-0001 (DODYCOEL), and Portuguese national funds, through the Fundacao para a Ciencia e a Tecnologia (Project FCT-ANR/BEX-BCM/0002/2013).; 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 d...


7 Resultados

Texto Pesquisado

Refinar resultados

Autor















Data





Tipo de Documento



Financiamento



Tipo de acesso


Recurso


Assunto