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Pesquisa : D08.811.682.662.171 [Categoria DeCS]
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[PMID]:28461337
[Au] Autor:Wang Y; Landry AP; Ding H
[Ad] Endereço:From the Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803.
[Ti] Título:The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH to oxygen or ubiquinone.
[So] Source:J Biol Chem;292(24):10061-10067, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Increasing evidence suggests that mitoNEET, a target of the type II diabetes drug pioglitazone, is a key regulator of energy metabolism in mitochondria. MitoNEET is anchored to the mitochondrial outer membrane via its N-terminal α helix domain and hosts a redox-active [2Fe-2S] cluster in its C-terminal cytosolic region. The mechanism by which mitoNEET regulates energy metabolism in mitochondria, however, is not fully understood. Previous studies have shown that mitoNEET specifically interacts with the reduced flavin mononucleotide (FMNH ) and that FMNH can quickly reduce the mitoNEET [2Fe-2S] clusters. Here we report that the reduced mitoNEET [2Fe-2S] clusters can be readily oxidized by oxygen. In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen. Ubiquinone-2, an analog of ubiquinone-10, can also oxidize the reduced mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions. Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria. Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.
[Mh] Termos MeSH primário: Mononucleotídeo de Flavina/metabolismo
Hidroquinonas/metabolismo
Membranas Mitocondriais/enzimologia
Proteínas Mitocondriais/metabolismo
Ubiquinona/metabolismo
[Mh] Termos MeSH secundário: Espectroscopia de Ressonância de Spin Eletrônica
Transporte de Elétrons/efeitos dos fármacos
Metabolismo Energético/efeitos dos fármacos
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
FMN Redutase/genética
FMN Redutase/metabolismo
Seres Humanos
Hipoglicemiantes/farmacologia
Cinética
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Oxirredução
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Tiazóis/farmacologia
Tiazolidinedionas/farmacologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5-(3,5-di-tert-butyl-4-hydroxybenzyl)-4-hydroxythiazol-2(5H)-one); 0 (CISD1 protein, human); 0 (Escherichia coli Proteins); 0 (Hydroquinones); 0 (Hypoglycemic Agents); 0 (Mitochondrial Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 0 (Thiazoles); 0 (Thiazolidinediones); 0 (flavin mononucleotide hydroquinone); 1339-63-5 (Ubiquinone); 7N464URE7E (Flavin Mononucleotide); EC 1.5.1.38 (FMN Reductase); EC 1.5.1.41 (Fre protein, E coli); I7T5V2W47R (Ubiquinone Q2); X4OV71U42S (pioglitazone)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.789800


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[PMID]:28452474
[Au] Autor:McDowall JS; Ntai I; Hake J; Whitley PR; Mason JM; Pudney CR; Brown DR
[Ad] Endereço:Department of Biology and Biochemistry, Faculty of Science, University of Bath , Bath, U.K.
[Ti] Título:Steady-State Kinetics of α-Synuclein Ferrireductase Activity Identifies the Catalytically Competent Species.
[So] Source:Biochemistry;56(19):2497-2505, 2017 05 16.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:α-Synuclein (α-syn) is a cytosolic protein known for its association with neurodegenerative diseases, including Parkinson's disease and other synucleinopathies. The potential cellular function of α-synuclein may be of consequence for understanding the pathogenesis of such diseases. Previous work has suggested that α-synuclein can catalyze the reduction of iron as a ferrireductase. We performed a detailed analysis of the steady-state kinetics of recombinant α-syn ferrireductase activity and for disease-associated variants. Our study illustrates that the ferrireductase activity we observed is clearly commensurate with bona fide enzyme activity and suggests a mechanistic rationale for the activity and the relationship to cellular regulation of the pool of Fe(III) and Fe(II). Using cell-based studies, we examined the functionally active conformation and found that the major catalytically active form is a putative membrane-associated tetramer. Using an artificial membrane environment with recombinant protein, we demonstrate that secondary structure folding of α-synuclein is insufficient to allow enzyme activity and the absolute specificity of the tertiary/quaternary structure is the primary requirement. Finally, we explored the steady-state kinetics of a range of disease α-synuclein variants and found that variants involved in neurodegenerative disease exhibited major changes in their enzymatic activity. We discuss these data in the context of a potential disease-associated mechanism for aberrant α-synuclein ferrireductase activity.
[Mh] Termos MeSH primário: FMN Redutase/metabolismo
Proteínas de Membrana/metabolismo
Modelos Biológicos
Proteínas do Tecido Nervoso/metabolismo
Neurônios/enzimologia
alfa-Sinucleína/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Sítios de Ligação
Biocatálise
Linhagem Celular Tumoral
FMN Redutase/química
FMN Redutase/genética
Seres Humanos
Lipossomos
Proteínas de Membrana/química
Proteínas de Membrana/genética
Peso Molecular
Mutação
Nanoestruturas/química
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Neurônios/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Especificidade por Substrato
alfa-Sinucleína/química
alfa-Sinucleína/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Liposomes); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Recombinant Proteins); 0 (alpha-Synuclein); EC 1.5.1.38 (FMN Reductase); EC 1.6.99.- (ferric citrate iron reductase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00257


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[PMID]:28673786
[Au] Autor:Zhang Y; Wan D; Zhou X; Long C; Wu X; Li L; He L; Huang P; Chen S; Tan B; Yin Y
[Ad] Endereço:Key Laboratory of Agro-Ecological Processes in Subtropical Region, Institute of Subtropical Agriculture, Chinese Academy of Sciences, National Engineering Laboratory for Pollution Control and Waste Utilization in Livestock and Poultry Production, Hunan Provincial Engineering Research Center for Heal
[Ti] Título:Diurnal variations in iron concentrations and expression of genes involved in iron absorption and metabolism in pigs.
[So] Source:Biochem Biophys Res Commun;490(4):1210-1214, 2017 Sep 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diurnal variations in serum iron levels have been well documented in clinical studies, and serum iron is an important diagnostic index for iron-deficiency anemia. However, the underlying mechanism of dynamic iron regulation in response to the circadian rhythm is still unclear. In this study, we investigated daily variations in iron status in the plasma and liver of pigs. The transcripts encoding key factors involved in iron uptake and homeostasis were evaluated. The results showed that iron levels in the plasma and liver exhibited diurnal rhythms. Diurnal variations were also observed in transcript levels of divalent metal transporter 1 (DMT1), membrane-associated ferric reductase 1 (DCYTB), and transferrin receptor (TfR) in the duodenum and jejunum, as well as hepcidin (HAMP) and TfR in the liver. Moreover, the results showed a network in which diurnal variations in systemic iron levels were tightly regulated by hepcidin and Tf/TfR via DCYTB and DMT1. These findings provide new insights into circadian iron homeostasis regulation. The diurnal variations in serum iron levels may also have pathophysiological implications for clinical diagnostics related to iron deficiency anemia in pigs.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/genética
Ritmo Circadiano/fisiologia
FMN Redutase/genética
Ferro/sangue
Ferro/metabolismo
Receptores da Transferrina/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte de Cátions/metabolismo
FMN Redutase/metabolismo
Fígado/química
Fígado/metabolismo
Receptores da Transferrina/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Receptors, Transferrin); 0 (solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2); E1UOL152H7 (Iron); EC 1.5.1.38 (FMN Reductase); EC 1.6.99.- (ferric citrate iron reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE


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[PMID]:28499769
[Au] Autor:Koch K; Hromic A; Sorokina M; Strandback E; Reisinger M; Gruber K; Macheroux P
[Ad] Endereço:Institute of Biochemistry, Graz University of Technology, Petersgasse 12/2, 8010 Graz, Austria.
[Ti] Título:Structure, biochemical and kinetic properties of recombinant Pst2p from Saccharomyces cerevisiae, a FMN-dependent NAD(P)H:quinone oxidoreductase.
[So] Source:Biochim Biophys Acta;1865(8):1046-1056, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The genome of the yeast Saccharomyces cerevisiae encodes four flavodoxin-like proteins, namely Lot6p, Pst2p, Rfs1p and Ycp4p. Thus far only Lot6p was characterized in detail demonstrating that the enzyme possesses NAD(P)H:quinone oxidoreductase activity. In the present study, we heterologously expressed PST2 in Escherichia coli and purified the produced protein to conduct a detailed biochemical and structural characterization. Determination of the three-dimensional structure by X-ray crystallography revealed that Pst2p adopts the flavodoxin-like fold and forms tetramers independent of cofactor binding. The lack of electron density for FMN indicated weak binding, which was confirmed by further biochemical analysis yielding a dissociation constant of 20±1µM. The redox potential of FMN bound to Pst2p was determined to -89±3mV and is thus 119mV more positive than that of free FMN indicating that reduced FMN binds ca. five orders of magnitude tighter to Pst2p than oxidized FMN. Due to this rather positive redox potential Pst2p is unable to reduce free FMN or azo dyes as reported for other members of the flavodoxin-like protein family. On the other hand, Pst2p efficiently catalyzes the NAD(P)H dependent two-electron reduction of natural and artificial quinones. The kinetic mechanism follows a ping-pong bi-bi reaction scheme. In vivo experiments with a PST2 knock out and overexpressing strain demonstrated that Pst2p enables yeast cells to cope with quinone-induced damage suggesting a role of the enzyme in managing oxidative stress.
[Mh] Termos MeSH primário: Benzoquinonas/metabolismo
FMN Redutase/metabolismo
NAD(P)H Desidrogenase (Quinona)/metabolismo
NADP/metabolismo
Proteínas Recombinantes/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cristalografia por Raios X/métodos
Escherichia coli/metabolismo
FMN Redutase/química
Mononucleotídeo de Flavina/metabolismo
Flavodoxina/metabolismo
Cinética
Modelos Moleculares
NAD/metabolismo
NAD(P)H Desidrogenase (Quinona)/química
Oxirredução
Proteínas Recombinantes/química
Proteínas de Saccharomyces cerevisiae/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Flavodoxin); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 0U46U6E8UK (NAD); 3T006GV98U (quinone); 53-59-8 (NADP); 7N464URE7E (Flavin Mononucleotide); EC 1.5.1.38 (FMN Reductase); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone))
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170514
[St] Status:MEDLINE


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[PMID]:28421437
[Au] Autor:Esimbekova EN; Nemtseva EV; Kirillova MA; Asanova AA; Kratasyuk VA
[Ad] Endereço:Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russia. esimbekova@yandex.ru.
[Ti] Título:Bioluminescent assay for toxicological assessment of nanomaterials.
[So] Source:Dokl Biochem Biophys;472(1):60-63, 2017 Jan.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:A new method for assessing biotoxicity of nanomaterials, based on the use of soluble bioluminescent coupled enzyme system NAD(P)â‹…H:FMN oxidoreductase and luciferase, is proposed. The results of this study indicate a significant adverse biological effect exerted by nanoparticles at the molecular level. It was found that the most toxic nanoparticles the nanoparticles are based on copper and copper oxide, as well as single-walled carbon nanotubes and multi-walled carbon nanofibers, which are referred to hazard class II.
[Mh] Termos MeSH primário: Medições Luminescentes/métodos
Nanopartículas Metálicas/toxicidade
Nanotubos de Carbono/toxicidade
Testes de Toxicidade/métodos
[Mh] Termos MeSH secundário: Cobre/química
FMN Redutase/química
Luciferases/química
Nanopartículas Metálicas/química
NADP/química
Nanotubos de Carbono/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nanotubes, Carbon); 53-59-8 (NADP); 789U1901C5 (Copper); EC 1.13.12.- (Luciferases); EC 1.5.1.38 (FMN Reductase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672917010173


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[PMID]:28345146
[Au] Autor:Tabib CR; Brodl E; Macheroux P
[Ad] Endereço:Institute of Biochemistry, Graz University of Technology, Petersgasse 12/II, A-8010, Graz, Austria.
[Ti] Título:Evidence for the generation of myristylated FMN by bacterial luciferase.
[So] Source:Mol Microbiol;104(6):1027-1036, 2017 Jun.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The genes responsible for the light production in bioluminescent bacteria are present as an operon, luxCDABEG. Many strains of Photobacteria carry an additional gene, termed luxF. X-ray crystallographic analysis of LuxF revealed the presence of four molecules of a flavin derivative, i.e. 6-(3'-(R)-myristyl) flavin adenine mononucleotide (myrFMN) non-covalently bound to the homodimer. In the present study, we exploited the binding of myrFMN to recombinant apo-LuxF to explore the occurrence of myrFMN in various bioluminescent bacteria. MyrFMN was detected in all bacterial strains tested including Vibrio and Aliivibrio indicating that it is more widely occurring in bioluminescent bacteria than previously assumed. We also show that apo-LuxF captures myrFMN and thereby relieves the inhibitory effect on luciferase activity. Thus our results provide support for the hypothesis that LuxF acts as a scavenger of myrFMN in bioluminescent bacteria. However, the source of myrFMN remained obscure. To address this issue, we established a cofactor regeneration enzyme-catalyzed cascade reaction that supports luciferase activity in vitro for up to 3 days. This approach enabled us to unambiguously demonstrate that myrFMN is generated in the bacterial bioluminescent reaction. Based on this finding we postulate a reaction mechanism for myrFMN generation that is based on the luciferase reaction.
[Mh] Termos MeSH primário: FMN Redutase/genética
Mononucleotídeo de Flavina/metabolismo
Luciferases Bacterianas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Cristalografia por Raios X
FMN Redutase/metabolismo
Mononucleotídeo de Flavina/química
Flavinas/metabolismo
Cinética
Luciferases/genética
Luciferases/metabolismo
Luciferases Bacterianas/genética
Óperon/genética
Oxirredução
Photobacterium/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavins); 7N464URE7E (Flavin Mononucleotide); EC 1.13.12.- (Luciferases); EC 1.14.14.3 (Luciferases, Bacterial); EC 1.14.14.3 (alkanol monooxygenase (FMN-linked)); EC 1.5.1.38 (FMN Reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13676


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[PMID]:28278216
[Au] Autor:Masuda H; Shimochi E; Hamada T; Senoura T; Kobayashi T; Aung MS; Ishimaru Y; Ogo Y; Nakanishi H; Nishizawa NK
[Ad] Endereço:Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.
[Ti] Título:A new transgenic rice line exhibiting enhanced ferric iron reduction and phytosiderophore production confers tolerance to low iron availability in calcareous soil.
[So] Source:PLoS One;12(3):e0173441, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Iron (Fe) deficiency is a critical agricultural problem, especially in calcareous soil, which is distributed worldwide. Rice plants take up Fe(II) from soil through a OsIRT1 transporter (Strategy I-related system) and also take up Fe(III) via a phytosiderophore-based system (Strategy II system). However, rice plants are susceptible to low-Fe conditions because they have low Fe(III) reduction activity and low-level phytosiderophore secretion. Previously, we produced transgenic rice plants expressing a mutationally reconstructed yeast ferric chelate reductase, refre1/372, under the control of the OsIRT1 promoter. This transgenic rice line exhibited higher Fe(III) chelate reductase activity and tolerance to Fe deficiency. In addition, we produced transgenic rice overexpressing the Fe deficiency-inducible transcription factor, OsIRO2, which regulates the expression of various genes involved in the strategy II Fe(III) uptake system, including OsNAS1, OsNAAT1, OsDMAS1, OsYSL15, and TOM1. This transgenic rice exhibited improved phytosiderophore secretion ability and tolerance to Fe deficiency. In the present research, transgenic rice plants that possess both the OsIRT1 promoter-refre1/372 and the 35S promoter-OsIRO2 (RI lines) were produced to enhance both Strategy I Fe(II) reductase ability and Strategy II phytosiderophore productivity. RI lines exhibited enhanced tolerance to Fe-deficient conditions at the early and middle-late stages of growth in calcareous soil, compared to both the non-transgenic line and lines harboring either OsIRT1 promoter-refre1/372 or 35S promoter-OsIRO2 alone. RI lines also exhibited a 9-fold higher yield than the non-transgenic line. Moreover, we successfully produced Fe-deficiency-tolerant Tachisugata rice, which is a high-biomass variety used as fodder. Collectively, our results demonstrate that combined enhancement of two Fe uptake systems in rice is highly effective in conferring tolerance to low Fe availability in calcareous soil.
[Mh] Termos MeSH primário: Carbonato de Cálcio/análise
Ferro/metabolismo
Oryza/genética
Oryza/metabolismo
Sideróforos/metabolismo
Solo/química
[Mh] Termos MeSH secundário: Biomassa
FMN Redutase/genética
FMN Redutase/metabolismo
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Ferro/farmacologia
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Oryza/efeitos dos fármacos
Oryza/enzimologia
Oxirredução
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Transport Proteins); 0 (Siderophores); 0 (Soil); E1UOL152H7 (Iron); EC 1.5.1.38 (FMN Reductase); EC 1.6.99.- (ferric citrate iron reductase); H0G9379FGK (Calcium Carbonate)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173441


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[PMID]:28012287
[Au] Autor:Qiu W; Dai J; Wang N; Guo X; Zhang X; Zuo Y
[Ad] Endereço:Key Laboratory of Plant-Soil Interactions, MOE, Centre for Resource, Environment and Food Security, China Agricultural University, Beijing 100193, China.
[Ti] Título:Effects of Fe-deficient conditions on Fe uptake and utilization in P-efficient soybean.
[So] Source:Plant Physiol Biochem;112:1-8, 2017 Mar.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Phosphorus (P)-efficient soybean (Glycine max) plants absorb and utilize P with high efficiency. To investigate the effects of iron (Fe)-deficient conditions on the absorption and utilization of Fe in P-efficient soybean plants, two soybean cultivars with different P efficiency, the 03-3 (P-efficient variety) and Bd-2 (P-inefficient variety), were used in this study. The two soybean cultivars were grown in nutrient solution containing Fe concentrations of 0 (Fe0), 20 (Fe20), 40 (Fe40), or 80 (Fe80) µM for 7 days. The Fe reductase activity of roots was higher in 03-3 plants grown under the Fe0, Fe20, and Fe40 treatments than in Bd-2 plants and the total Fe uptake was greater in 03-3 plants under the Fe40 treatment. GmFRD3a was much more highly expressed in the stem of 03-3 than in that of Bd-2, and significantly more iron was transported to 03-3 plant shoots during Fe0 treatment. Chlorosis in young leaves caused by Fe deficiency under the Fe0 and Fe20 treatments was alleviated by increased Fe concentration in shoots. Increased levels of active Fe in young 03-3 leaves under Fe-deprivation conditions (Fe0) and maintenance of stable Fe concentrations in 03-3 shoots subjected to Fe20, Fe40, and Fe80 treatments suggested that the P-efficient 03-3 cultivar is also Fe-efficient. It is suggested that 03-3 soybean cultivar should be a good resource for application to farm field.
[Mh] Termos MeSH primário: Ferro/metabolismo
Fósforo/metabolismo
Feijão de Soja/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Biomassa
FMN Redutase/metabolismo
Regulação da Expressão Gênica de Plantas
Ferro/farmacologia
Folhas de Planta/efeitos dos fármacos
Folhas de Planta/metabolismo
Raízes de Plantas/efeitos dos fármacos
Raízes de Plantas/metabolismo
Brotos de Planta/metabolismo
Solo
Feijão de Soja/genética
Feijão de Soja/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Soil); 27YLU75U4W (Phosphorus); E1UOL152H7 (Iron); EC 1.5.1.38 (FMN Reductase); EC 1.6.99.- (ferric citrate iron reductase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


  9 / 662 MEDLINE  
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[PMID]:27919686
[Au] Autor:Kim H; Chaurasia AK; Kim T; Choi J; Ha SC; Kim D; Kim KK
[Ad] Endereço:Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, Gyeonggi 16419, South Korea.
[Ti] Título:Structural and functional study of ChuY from Escherichia coli strain CFT073.
[So] Source:Biochem Biophys Res Commun;482(4):1176-1182, 2017 Jan 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The uropathogenic Escherichia coli strain CFT073 contains multiple iron and heme transport systems, which facilitate infection of the host urinary tract. To elucidate the molecular and cellular function of ChuY, a hypothetical gene in the heme degradation/utilization pathway, we solved the crystal structure of ChuY at 2.4 Å resolution. ChuY has high structural homology with human biliverdin and flavin reductase. We confirmed that ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. A chuY deletion-insertion strain showed reduced survival potential compared to wild-type and complemented strains in mammalian cells. Current results suggest ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of E. coli CFT073.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo
[Mh] Termos MeSH secundário: Animais
Biliverdina/química
Cristalografia por Raios X
Escherichia coli/patogenicidade
Proteínas de Escherichia coli/química
FMN Redutase/química
Deleção de Genes
Genômica
Células HEK293
Heme/química
Hemina/química
Homeostase
Seres Humanos
Ferro/química
Camundongos
NADP/química
Porfirinas/química
Conformação Proteica
Estrutura Secundária de Proteína
Células RAW 264.7
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Porphyrins); 42VZT0U6YR (Heme); 53-59-8 (NADP); 743LRP9S7N (Hemin); E1UOL152H7 (Iron); EC 1.3.- (ChuY protein, E coli); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.5.1.38 (FMN Reductase); EC 1.5.1.41 (Fre protein, E coli); O9MIA842K9 (Biliverdine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE


  10 / 662 MEDLINE  
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[PMID]:27806563
[Au] Autor:Musila JM; Ellis HR
[Ad] Endereço:Department of Chemistry and Biochemistry, Auburn University , Auburn, Alabama 36849, United States.
[Ti] Título:Transformation of a Flavin-Free FMN Reductase to a Canonical Flavoprotein through Modification of the π-Helix.
[So] Source:Biochemistry;55(46):6389-6394, 2016 Nov 22.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The flavin reductase of the alkanesulfonate monooxygenase system (SsuE) contains a conserved π-helix located at the tetramer interface that originates from the insertion of Tyr118 into helix α4 of SsuE. Although the presence of π-helices provides an evolutionary gain of function, the defined role of these discrete secondary structures remains largely unexplored. The Tyr118 residue that generated the π-helix in SsuE was substituted with Ala to evaluate the functional role of this distinctive structural feature. Interestingly, generation of the Y118A SsuE variant converted the typically flavin-free enzyme to a flavin-bound form. Mass spectrometric analysis of the extracted flavin gave a mass of 457.11 similar to that of the FMN cofactor, suggesting the Y118A SsuE variant retained flavin specificity. The Y118A SsuE FMN cofactor was reduced with approximately 1 equiv of NADPH in anaerobic titration experiments, and the flavin remained bound following reduction. Although reactivity of the reduced flavin with oxygen was slow in NADPH oxidase assays, the variant supported electron transfer to ferricyanide. In addition, there was no measurable sulfite product in coupled assays with the Y118A SsuE variant and SsuD, further demonstrating that flavin transfer was no longer supported. The results from these studies suggest that the π-helix enables SsuE to effectively utilize flavin as a substrate in the two-component monooxygenase system and provides a foundation for further studies aimed at evaluating the functional properties of the π-helix in SsuE and related two-component flavin reductase enzymes.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
FMN Redutase/química
Flavinas/química
Flavoproteínas/química
Estrutura Secundária de Proteína
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Dicroísmo Circular
FMN Redutase/genética
FMN Redutase/metabolismo
Flavinas/metabolismo
Flavoproteínas/genética
Flavoproteínas/metabolismo
Ligações de Hidrogênio
Cinética
Modelos Moleculares
Mutação
Ligação Proteica
Domínios Proteicos
Espectrofotometria
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavins); 0 (Flavoproteins); EC 1.5.1.38 (FMN Reductase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE



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