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drug target
the cytotoxicity of heteroaromatic N-oxides in murine hepatoma MH22a and human colon carcinoma HCT-116 cells increases with the geometric average of their reactivity towards NADPH:cytochrome P-450 reductase and Plasmodium falciparum ferredoxin:NADP+ oxidoreductase, and with their reactivity towards rat NQO1
evolution
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NfnA architecturally belongs to the Fnr family, while NfnB is a member of a disulfide oxidoreductase superfamily
evolution
the enzyme is a member of the flavoprotein superfamily
evolution
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the enzyme is a member of the flavoprotein superfamily
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metabolism
FNR mediates the final step of photosynthetic electron flow by transferring electrons from ferredoxin to NADP+
metabolism
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function in ferric iron metabolism
metabolism
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
metabolism
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
metabolism
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
metabolism
the enzyme also drives the Fenton reaction
metabolism
the petH gene encoding ferredoxin:NADP+ oxidoreductase has two translation products depending on growth conditions and leading to two isoforms. Under standard conditions where FNRL accumulates, two transcriptional start points are found at -52 and -34 relative to the first translation start site. Under nitrogen-starvation conditions where FNRS accumulates a transcriptional start point is mapped at -126 relative to the first translation start site. Therefore, the transcript responsible for FNRS translation is longer than that producing FNRL
metabolism
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the enzyme has a function in utilizing any excess reducing power of NADPH
metabolism
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function in ferric iron metabolism
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physiological function
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ferredoxin and Fd-NADP+ reductase are redox partners responsible for the conversion between NADP+ and NADPH in the plastids of photosynthetic organisms
physiological function
FNR associated with the cytochrome b6f complex can participate in the cyclic electron transport as photosystem I-plastoquinone or NADPH-plastoquinone oxidoreductase
physiological function
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FNR catalyses the ferredoxin-dependent reduction of NADP+ to NADPH in linear photosynthetic electron transport. The enzyme also transfers electrons from reduced ferredoxin or NADPH to the cytochrome b6f complex in cyclic electron transport
physiological function
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FNR catalyses the ferredoxin-dependent reduction of NADP+ to NADPH in linear photosynthetic electron transport. The enzyme also transfers electrons from reduced ferredoxin or NADPH to the cytochrome b6f complex in cyclic electron transport
physiological function
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FNR catalyzes the final step of the linear photosynthetic electron flow by mediating the electron transfer from reduced ferredoxin to NADP+ with formation of NADPH for CO2 assimilation or other biosynthetic pathways. This process is a rate-limiting step of photosynthesis under both limiting and saturating light conditions. FNR is also involved in the cyclic electron flow around photosystem I, cyclic PSI, by its photoproduct NADPH recycling to plastoquinone or the cytochrome b6f complex. Analysis of contribution of FNR and NDH-1 to cyclic PSI under low CO2 conditions, overview
physiological function
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FNR mediates the redox reaction between NADP+/NADPH and ferredoxin, providing redox equivalents in cell-material synthesis
physiological function
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in chloroplasts and cyanobacteria, FNR provides the NADPH necessary for photosynthetic CO2 assimilation
physiological function
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in the photosystem I, an oxidized ferredoxin molecule, Fdox, first receives an electron driven by light energy to form a reduced ferredoxin, Fdred. The FAD-containing FNR then catalyzes the transfer of the electron to NADP+, which recycles Fdred back to Fdox. On the other hand, FNR mainly catalyzes the conversion from Fdox to Fdred in reactions other than photosynthesis
physiological function
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the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
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the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
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the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
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the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview
physiological function
enzyme associated with the cytochrome b6f complex can participate in the cyclic electron transport in the chloroplast as photosystem I-plastoquinone or NADPH-plastoquinone oxidoreductase. Ferredoxin is not directly required for plastoquinone reduction but is rather necessary for the reduction of ferredoxin reductase under light conditions during operation of the cyclic electron transport
physiological function
enzyme is able to substitute for the ferredoxin-NADP+-reductase in Escherichia coli in its antioxidant role. It is involved in the oxidative stress response of Xanthomonas axonopodis pv. citri and performs its biological function most likely through the interaction with ferredoxin XAC1762
physiological function
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ferredoxin-ferredoxin reductase binding is accompanied by endothermic reactions and driven by the entropy gain. Increases in the conformational entropy of the ferredoxin-ferredoxin reductase complex contribute largely to stabilizing the complex. Ferredoxin binding leads to both structural stiffening and softening of ferredoxin reductase. Enhanced ferredoxin reductase backbone fluctuations suggest favorable contributions to the net conformational entropy. Relatively large-scale motions of the C-terminus, a gatekeeper for interactions of NADP(H), are quenched in the closed form, thereby facilitating exit of NADP(H)
physiological function
ferredoxin:NADP+-oxidoreductase-mediated NADPH production limits the efficient hydrogen production by [FeFe]-hydrogenase HydA in both purified photosystem I and isolated thylakoids. Ferredoxin:NADP+-oxidoreductase is physically bound to the photosynthetic membrane in both plant and algal thylakoids. Exogenous ferredoxin:NADP+-oxidoreductase is able to form a tight-binding complex with photosystem I. Replacing the hydrogenase with a ferredoxin-hydrogenase fusion switches the bias of electron transfer from the enzyme to the hydrogenase and results in an increased rate of hydrogen photoproduction
physiological function
Phe256, which is important for binding to ferredoxin, and Lys259 are the crucial residues for electron transfer with ferredoxin
physiological function
Escherichia coli cells deficient in the soxRS-induced ferredoxin (flavodoxin)-NADP(H) reductase FPR, display abnormal sensitivity to methyl viologen. Neither bacteriostatic effects nor inactivation of oxidant-sensitive hydrolyases can be detected in mutant cells exposed to methyl viologen. FPR inactivation does not affect the methyl viologen-driven soxRS response, FPR overexpression leads to enhanced stimulation of the regulon, with concomitant oxidation of the NADPH pool. Accumulation of a site-directed FPR mutant that uses NAD(H) instead of NADP(H) has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
physiological function
insertion mutants lacking a functional enzyme do not require methionine and grow well anaerobically, but they show increased sensitivity to paraquat
physiological function
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the enzyme has a major role in reduction of toxic nitrite in roots
physiological function
the enzyme is important for growth in the presence of sulfur
physiological function
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the enzyme is required for the growth of Pseudomonas aeruginosa
physiological function
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the enzyme plays a central role in chloroplast redox metabolism. Thylakoid-bound enzyme activity decreases while excess soluble enzyme increases superoxide radical production in the light
physiological function
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in the photosystem I, an oxidized ferredoxin molecule, Fdox, first receives an electron driven by light energy to form a reduced ferredoxin, Fdred. The FAD-containing FNR then catalyzes the transfer of the electron to NADP+, which recycles Fdred back to Fdox. On the other hand, FNR mainly catalyzes the conversion from Fdox to Fdred in reactions other than photosynthesis
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physiological function
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Phe256, which is important for binding to ferredoxin, and Lys259 are the crucial residues for electron transfer with ferredoxin
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physiological function
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the enzyme is important for growth in the presence of sulfur
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physiological function
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the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview
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additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery
additional information
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FNR interacts with Tic62, a member of the Tic complex, i.e. translocon at the inner envelope of chloroplasts, involved in redox-regulation of protein import into chloroplasts. Tic62 represents a major FNR interaction protein partner at the thylakoids, and binding to Tic62 clearly increases the stability of FNR. The specific interaction with FNR is mediated by a conserved sequence motif rich in proline and serine residues, located in the C terminus of Tic62
additional information
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introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins results in 13 different Fd-FNR cross-linked complexes displaying a broad range of activity to catalyze the NADPH-dependent cytochrome c reduction
additional information
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the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast
additional information
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the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast
additional information
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the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast. In Arabidopsis mutants completely devoid of FNR1 or FNR2 all high molecular weight FNR complexes are absent
additional information
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the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast. Nicotiana tabacum mutants with inactivated ndh genes show no reduction in the accumulation of FNR at the thylakoid membrane
additional information
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titration behaviour of Glu312, overview
additional information
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while in the wild-type, vibrational enhanced modulation of the active site contributes to the tunnel probability of hydride transfer, complexes of some of the active site mutants with the coenzyme hardly allow the relative movement of isoalloxazine and nicotinamide rings along the hydride transfer reaction. The architecture of the wild-type FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient hydride transfer processes