Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems
Distinct isoforms of FAD-containing ferredoxin-NADP<sup>+</sup> 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-electron transfer reactions...
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MDPI AG
2022-10-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/11/11/2143 |
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| author | Takashi Iyanagi |
| author_facet | Takashi Iyanagi |
| author_sort | Takashi Iyanagi |
| collection | DOAJ |
| description | Distinct isoforms of FAD-containing ferredoxin-NADP<sup>+</sup> 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-electron transfer reactions in steps involving FAD semiquinone intermediates. In cyanobacteria and some algae, one-electron carrier Fd serves as a substitute for low-potential FMN-containing flavodoxin (Fld) during growth under low-iron conditions. This complex evolves into the covalent FNR (FAD)-Fld (FMN) pair, which participates in a wide variety of NAD(P)H-dependent metabolic pathways as an electron donor, including bacterial sulfite reductase, cytochrome P450 BM3, plant or mammalian cytochrome P450 reductase and nitric oxide synthase isoforms. These electron transfer systems share the conserved Ser-Glu/Asp pair in the active site of the FAD module. In addition to physiological electron acceptors, the NAD(P)H-dependent diflavin reductase family catalyzes a one-electron reduction of artificial electron acceptors such as quinone-containing anticancer drugs. Conversely, NAD(P)H: quinone oxidoreductase (NQO1), which shares a Fld-like active site, functions as a typical two-electron transfer antioxidant enzyme, and the NQO1 and UDP-glucuronosyltransfease/sulfotransferase pairs function as an antioxidant detoxification system. In this review, the roles of the plant FNR-Fd and FNR-Fld complex pairs were compared to those of the diflavin reductase (FAD-FMN) family. In the final section, evolutionary aspects of NAD(P)H-dependent multi-domain electron transfer systems are discussed. |
| first_indexed | 2024-03-09T19:19:11Z |
| format | Article |
| id | doaj.art-86157034bb09433ca42d95b728028ae9 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-09T19:19:11Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-86157034bb09433ca42d95b728028ae92023-11-24T03:29:55ZengMDPI AGAntioxidants2076-39212022-10-011111214310.3390/antiox11112143Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer SystemsTakashi Iyanagi0Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Akoh 678-1297, Hyogo, JapanDistinct isoforms of FAD-containing ferredoxin-NADP<sup>+</sup> 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-electron transfer reactions in steps involving FAD semiquinone intermediates. In cyanobacteria and some algae, one-electron carrier Fd serves as a substitute for low-potential FMN-containing flavodoxin (Fld) during growth under low-iron conditions. This complex evolves into the covalent FNR (FAD)-Fld (FMN) pair, which participates in a wide variety of NAD(P)H-dependent metabolic pathways as an electron donor, including bacterial sulfite reductase, cytochrome P450 BM3, plant or mammalian cytochrome P450 reductase and nitric oxide synthase isoforms. These electron transfer systems share the conserved Ser-Glu/Asp pair in the active site of the FAD module. In addition to physiological electron acceptors, the NAD(P)H-dependent diflavin reductase family catalyzes a one-electron reduction of artificial electron acceptors such as quinone-containing anticancer drugs. Conversely, NAD(P)H: quinone oxidoreductase (NQO1), which shares a Fld-like active site, functions as a typical two-electron transfer antioxidant enzyme, and the NQO1 and UDP-glucuronosyltransfease/sulfotransferase pairs function as an antioxidant detoxification system. In this review, the roles of the plant FNR-Fd and FNR-Fld complex pairs were compared to those of the diflavin reductase (FAD-FMN) family. In the final section, evolutionary aspects of NAD(P)H-dependent multi-domain electron transfer systems are discussed.https://www.mdpi.com/2076-3921/11/11/2143ferredoxin-NADP<sup>+</sup> oxidoreductase (FNR)ferredoxin (Fd)flavodoxin (Fld)diflavin reductase familycatalytic cycleelectron transfer |
| spellingShingle | Takashi Iyanagi Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems Antioxidants ferredoxin-NADP<sup>+</sup> oxidoreductase (FNR) ferredoxin (Fd) flavodoxin (Fld) diflavin reductase family catalytic cycle electron transfer |
| title | Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems |
| title_full | Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems |
| title_fullStr | Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems |
| title_full_unstemmed | Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems |
| title_short | Roles of Ferredoxin-NADP<sup>+</sup> Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems |
| title_sort | roles of ferredoxin nadp sup sup oxidoreductase and flavodoxin in nad p h dependent electron transfer systems |
| topic | ferredoxin-NADP<sup>+</sup> oxidoreductase (FNR) ferredoxin (Fd) flavodoxin (Fld) diflavin reductase family catalytic cycle electron transfer |
| url | https://www.mdpi.com/2076-3921/11/11/2143 |
| work_keys_str_mv | AT takashiiyanagi rolesofferredoxinnadpsupsupoxidoreductaseandflavodoxininnadphdependentelectrontransfersystems |