Výsledky vyhledávání - "diflavin reductase"

Akademický článek

Roles of Ferredoxin-NADP+ Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems

Autor: Takashi Iyanagi

Publikováno v: Antioxidants, Vol 11, Iss 11, p 2143 (2022)

Distinct isoforms of FAD-containing ferredoxin-NADP+ oxidoreductase (FNR) and ferredoxin (Fd) are involved in photosynthetic and non-photosynthetic electron transfer systems. The FNR (FAD)-Fd [2Fe-2S] redox pair complex switches between one- and two-

Externí odkaz: https://doaj.org/article/86157034bb09433ca42d95b728028ae9

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Akademický článek

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Akademický článek

Correction: The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength

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

Publikováno v: Frontiers in Pharmacology, Vol 9 (2018)

Externí odkaz: https://doaj.org/article/d0cd274b52a4418d9e0aa7aee26dcca0

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Akademický článek

The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength

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

Publikováno v: Frontiers in Pharmacology, Vol 8 (2017)

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

Externí odkaz: https://doaj.org/article/f1ca40c81625441f975697aa2d133102

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The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength

Autor: Michel Kranendonk, Sophie Bozonnet, Thomas Lautier, Diana Campelo, Gilles Truan, Francisco de Assis Esteves, Philippe Urban

Publikováno v: Frontiers in Pharmacology
Frontiers in Pharmacology, 2017, 8, 13 p. ⟨10.3389/fphar.2017.00755⟩
Frontiers in Pharmacology, Frontiers, 2017, 8, 13 p. ⟨10.3389/fphar.2017.00755⟩
Frontiers in Pharmacology (8), 13 p.. (2017)
Frontiers in Pharmacology, Vol 8 (2017)

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)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09b3335f8a80ea77e7afc29570ecf298
https://hal.science/hal-01886446

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Fusion to Hydrophobin HFBI Improves the Catalytic Performance of a Cytochrome P450 System

Autor: Marco Girhard, Daniel Raszkowski, Vlada B. Urlacher, Dominik Schumacher, Sebastian Schulz

Publikováno v: Frontiers in Bioengineering and Biotechnology

Cytochrome P450 monooxygenases (P450) are heme-containing enzymes that oxidize a broad range of substrates in the presence of molecular oxygen and NAD(P)H. For their activity, most P450s rely on one or two redox proteins responsible for the transfer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::add0f984c467e2d2852e0468fbf95357
https://pubmed.ncbi.nlm.nih.gov/27458582

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