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Reaction Mechanism of the Ferredoxin–Ferredoxin NAD(P)+/H Oxidoreductase System

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A special issue of Antioxidants (ISSN 2076-3921).

Deadline for manuscript submissions: closed (15 December 2021) | Viewed by 10983

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Special Issue Editors

Dr. Daisuke Seo

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Guest Editor

Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan
Interests: ferredoxin-NAD(P)+ oxidoreductase; iron–sulfur protein; flavodoxin; cyctochrome c; phototrophic bacteria; iron–sulfur-type photoreaction center

Prof. Dr. Narimantas K. Cenas

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Co-Guest Editor

Institute of Biochemistry of Vilnius University, Saulėtekio 7, LT-10257 Vilnius, Lithuania
Interests: flavoenzyme catalysis; oxidative stress; bioreductive activation; redox active drugs; quinones; aromatic nitrocompounds and N-oxides; polyphenols
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Special Issue Information

Dear Colleagues,

Ferredoxin (Fd) and flavodoxin (Fld) function as an electron mediator in biosynthetic/biodegrading processes such as carbon dioxide assimilation, nitrogen assimilation, cytochrome P450-dependent oxygenation, and S-adenosylmethionine-dependent reactions. Fd and Fld are also involved in the generation and scavenging of reactive oxygen species as the nature of a low redox potential electron mediator. In many living organisms, ferredoxin-NAD(P)⁺ oxidoreductase (FNR) promotes Fd/Fld reduction/oxidation reactions in an NAD(P)⁺/H-dependent manner. Recent progress in genomics, proteomics, and metabolomics, as well as research with biochemical, biophysical, and physiological approaches to wide-ranging organisms, have expanded the versatility of the roles and reaction mechanisms of FNR and Fd-FNR systems.

This Special Issue invites research findings and reviews of recent works which share updates on and enrich our knowledge around FNRs, its isozymes, such as adrenodoxin reductase, putidaredoxin reductase, and its homologues, and Fd/Fld–FNR systems in bacteria, archaea, protozoa, plants, and vertebrate. The issue targets research on a molecular to cellular level: reaction intermediate, electron/hydride transfer reactions, substrate recognition, structure–function relation, supramolecular assembly, response to environmental and drug stresses utilizing spectroscopic, kinetic, and structural analyses, computational science, genomics, proteomics, and metabolomics approaches. We believe that this Special Issue, “Reaction Mechanism of a Ferredoxin–Ferredoxin NAD(P)⁺/H Oxidoreductase System”, will help to highlight the most recent advances on all aspects of Fd–FNR systems.

We look forward to your contribution.

Dr. Daisuke Seo
Prof. Dr. Narimantas K. Cenas
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antioxidants is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

Iron–sulfur protein
Flavodoxin
Adrenodoxin
Putidaredoxin
Flavin
NADH
NADPH
Oxidoreductase

Published Papers (4 papers)

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Research

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14 pages, 2000 KiB

Open AccessArticle

Thioredoxin Reductase-Type Ferredoxin: NADP⁺ Oxidoreductase of Rhodopseudomonas palustris: Potentiometric Characteristics and Reactions with Nonphysiological Oxidants

by Mindaugas Lesanavičius, Daisuke Seo and Narimantas Čėnas

Antioxidants 2022, 11(5), 1000; https://doi.org/10.3390/antiox11051000 - 19 May 2022

Viewed by 1559

Abstract

Rhodopseudomonas palustris ferredoxin:NADP⁺ oxidoreductase (RpFNR) belongs to a novel group of thioredoxin reductase-type FNRs with partly characterized redox properties. Based on the reactions of RpFNR with the 3-acetylpyridine adenine dinucleotide phosphate redox couple, we estimated the two-electron reduction midpoint potential of the FAD cofactor to be −0.285 V. 5-Deaza-FMN-sensitized photoreduction revealed −0.017 V separation of the redox potentials between the first and second electron transfer events. We examined the mechanism of oxidation of RpFNR by several different groups of nonphysiological electron acceptors. The k_cat/K_m values of quinones and aromatic N-oxides toward RpFNR increase with their single-electron reduction midpoint potential. The lower reactivity, mirroring their lower electron self-exchange rate, is also seen to have a similar trend for nitroaromatic compounds. A mixed single- and two-electron reduction was characteristic of quinones, with single-electron reduction accounting for 54% of the electron flux, whereas nitroaromatics were reduced exclusively via single-electron reduction. It is highly possible that the FADH· to FAD oxidation reaction is the rate-limiting step during the reoxidation of reduced FAD. The calculated electron transfer distances in the reaction with quinones and nitroaromatics were close to those of Anabaena and Plasmodium falciparum FNRs, thus demonstrating their similar “intrinsic” reactivity. Full article

(This article belongs to the Special Issue Reaction Mechanism of the Ferredoxin–Ferredoxin NAD(P)+/H Oxidoreductase System)

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20 pages, 3504 KiB

Open AccessArticle

Nanomechanical Study of Enzyme: Coenzyme Complexes: Bipartite Sites in Plastidic Ferredoxin-NADP⁺ Reductase for the Interaction with NADP⁺

by Sandra Pérez-Domínguez, Silvia Caballero-Mancebo, Carlos Marcuello, Marta Martínez-Júlvez, Milagros Medina and Anabel Lostao

Antioxidants 2022, 11(3), 537; https://doi.org/10.3390/antiox11030537 - 11 Mar 2022

Cited by 19 | Viewed by 3561

Abstract

Plastidic ferredoxin-NADP⁺ reductase (FNR) transfers two electrons from two ferredoxin or flavodoxin molecules to NADP⁺, generating NADPH. The forces holding the Anabaena FNR:NADP⁺ complex were analyzed by dynamic force spectroscopy, using WT FNR and three C-terminal Y303 variants, Y303S, Y303F, and Y303W. FNR was covalently immobilized on mica and NADP⁺ attached to AFM tips. Force–distance curves were collected for different loading rates and specific unbinding forces were analyzed under the Bell–Evans model to obtain the mechanostability parameters associated with the dissociation processes. The WT FNR:NADP⁺ complex presented a higher mechanical stability than that reported for the complexes with protein partners, corroborating the stronger affinity of FNR for NADP⁺. The Y303 mutation induced changes in the FNR:NADP⁺ interaction mechanical stability. NADP⁺ dissociated from WT and Y303W in a single event related to the release of the adenine moiety of the coenzyme. However, two events described the Y303S:NADP⁺ dissociation that was also a more durable complex due to the strong binding of the nicotinamide moiety of NADP⁺ to the catalytic site. Finally, Y303F shows intermediate behavior. Therefore, Y303, reported as crucial for achieving catalytically competent active site geometry, also regulates the concerted dissociation of the bipartite nucleotide moieties of the coenzyme. Full article

(This article belongs to the Special Issue Reaction Mechanism of the Ferredoxin–Ferredoxin NAD(P)+/H Oxidoreductase System)

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10 pages, 1802 KiB

Open AccessArticle

Effect of Artemisinin on the Redox System of NADPH/FNR/Ferredoxin from Malaria Parasites

by Yoko Kimata-Ariga and Rena Morihisa

Antioxidants 2022, 11(2), 273; https://doi.org/10.3390/antiox11020273 - 29 Jan 2022

Cited by 4 | Viewed by 1919

Abstract

FNR and ferredoxin constitute a redox cascade, which provides reducing power in the plastid of malaria parasites. Recently, mutation of ferredoxin (D97Y) was reported to be strongly related to the parasite’s resistance to the front-line antimalarial drug artemisinin. In order to gain insight into the mechanism for the resistance, we studied the effect of dihydroartemisinin (DHA), the active compound of artemisinin, on the redox cascade of NADPH/FNR/ferredoxin in in vitro reconstituted systems. DHA partially inhibited the diaphorase activity of FNR by decreasing the affinity of FNR for NADPH. The activity of the electron transfer from FNR to wild-type or D97Y mutant ferredoxin was not significantly affected by DHA. An in silico docking analysis indicated possible binding of DHA molecule in the binding cavity of 2′5′ADP, a competitive inhibitor for NADPH, on FNR. We previously showed that the D97Y mutant of ferredoxin binds to FNR more strongly than wild-type ferredoxin, and ferredoxin and FNR are generally known to be involved in the oxidative stress response. Thus, these results suggest that ferredoxin is not a direct target of artemisinin, but its mutation may be involved in the protective response against the oxidative stress caused by artemisinin. Full article

(This article belongs to the Special Issue Reaction Mechanism of the Ferredoxin–Ferredoxin NAD(P)+/H Oxidoreductase System)

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Review

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25 pages, 4882 KiB

Open AccessReview

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

by Takashi Iyanagi

Antioxidants 2022, 11(11), 2143; https://doi.org/10.3390/antiox11112143 - 29 Oct 2022

Cited by 6 | Viewed by 3086

Abstract

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-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. Full article

(This article belongs to the Special Issue Reaction Mechanism of the Ferredoxin–Ferredoxin NAD(P)+/H Oxidoreductase System)

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