Base de dados : MEDLINE
Pesquisa : D08.811.682.608.800 [Categoria DeCS]
Referências encontradas : 1492 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 150 ir para página                         

  1 / 1492 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28687205
[Au] Autor:Zaryanova EV; Lozinskaya NA; Beznos OV; Volkova MS; Chesnokova NB; Zefirov NS
[Ad] Endereço:Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia. Electronic address: atashi-akane@mail.ru.
[Ti] Título:Oxindole-based intraocular pressure reducing agents.
[So] Source:Bioorg Med Chem Lett;27(16):3787-3793, 2017 08 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The study represents the new findings at the crossroads of chemistry and medicine, particularly between medicinal and organic chemistry and ophthalmology. In this work we describe how the chemical reactivity of indolinone scaffold may be used to create small molecule ligands with strong biological response comparable with and larger than that of endogenous hormone. The synthesis of oxindole-based melatonin and 5-methoxycarbonylamino-N-acetyltryptamine (5-MCA-NAT) analogues was proposed and their ability to influence intraocular pressure (IOP) was studied in vivo. Time-dependent study revealed the prolonged effect (more than 6h) of the lead-compound. This effect in combination with high IOP reducing effect (41±6%) in low concentrations of the active compound (0.1wt%) and with high water solubility represents a great potential of low-cost oxindole derivatives as potent antiglaucoma agents.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Indóis/farmacologia
Pressão Intraocular/efeitos dos fármacos
Quinona Redutases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Seres Humanos
Indóis/síntese química
Indóis/química
Ligantes
Modelos Moleculares
Estrutura Molecular
Quinona Redutases/metabolismo
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Indoles); 0 (Ligands); 0S9338U62H (2-oxindole); EC 1.6.99.- (NRH - quinone oxidoreductase2); EC 1.6.99.- (Quinone Reductases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE


  2 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28684420
[Au] Autor:Motl N; Skiba MA; Kabil O; Smith JL; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600 and.
[Ti] Título:Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.
[So] Source:J Biol Chem;292(34):14026-14038, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation pathway, which comprises sulfide quinone oxidoreductase, persulfide dioxygenase (PDO), rhodanese, and sulfite oxidase and converts H S to thiosulfate and sulfate. Natural fusions between the non-heme iron containing PDO and rhodanese, a thiol sulfurtransferase, exist in some bacteria. However, little is known about the role of the PDO-rhodanese fusion (PRF) proteins in sulfur metabolism. Herein, we report the kinetic properties and the crystal structure of a PRF from the Gram-negative endophytic bacterium The crystal structures of wild-type PRF and a sulfurtransferase-inactivated C314S mutant with and without glutathione were determined at 1.8, 2.4, and 2.7 Å resolution, respectively. We found that the two active sites are distant and do not show evidence of direct communication. The PRF exhibited robust PDO activity and preferentially catalyzed sulfur transfer in the direction of thiosulfate to sulfite and glutathione persulfide; sulfur transfer in the reverse direction was detectable only under limited turnover conditions. Together with the kinetic data, our bioinformatics analysis reveals that PRF is poised to metabolize thiosulfate to sulfite in a sulfur assimilation pathway rather than in sulfide stress response as seen, for example, with the PRF or sulfide oxidation and disposal as observed with the homologous mammalian proteins.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Burkholderiaceae/enzimologia
Modelos Moleculares
Proteínas Mutantes Quiméricas/metabolismo
Quinona Redutases/metabolismo
Tiossulfato Sulfurtransferase/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Biologia Computacional
Cristalografia por Raios X
Cisteína/química
Dissulfetos/metabolismo
Estabilidade Enzimática
Glutationa/análogos & derivados
Glutationa/química
Glutationa/metabolismo
Sulfeto de Hidrogênio/metabolismo
Proteínas Mutantes Quiméricas/química
Proteínas Mutantes Quiméricas/genética
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Quinona Redutases/química
Quinona Redutases/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Tiossulfato Sulfurtransferase/química
Tiossulfato Sulfurtransferase/genética
Tiossulfatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Disulfides); 0 (Mutant Chimeric Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 0 (Thiosulfates); 0 (glutathione persulfide); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.790170


  3 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28415976
[Au] Autor:Elghraoui A; Modlin SJ; Valafar F
[Ad] Endereço:Biological and Medical Informatics Research Center, San Diego State University, Campanile Drive, San Diego, 92182, USA.
[Ti] Título:SMRT genome assembly corrects reference errors, resolving the genetic basis of virulence in Mycobacterium tuberculosis.
[So] Source:BMC Genomics;18(1):302, 2017 04 17.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The genetic basis of virulence in Mycobacterium tuberculosis has been investigated through genome comparisons of virulent (H37Rv) and attenuated (H37Ra) sister strains. Such analysis, however, relies heavily on the accuracy of the sequences. While the H37Rv reference genome has had several corrections to date, that of H37Ra is unmodified since its original publication. RESULTS: Here, we report the assembly and finishing of the H37Ra genome from single-molecule, real-time (SMRT) sequencing. Our assembly reveals that the number of H37Ra-specific variants is less than half of what the Sanger-based H37Ra reference sequence indicates, undermining and, in some cases, invalidating the conclusions of several studies. PE_PPE family genes, which are intractable to commonly-used sequencing platforms because of their repetitive and GC-rich nature, are overrepresented in the set of genes in which all reported H37Ra-specific variants are contradicted. Further, one of the sequencing errors in H37Ra masks a true variant in common with the clinical strain CDC1551 which, when considered in the context of previous work, corresponds to a sequencing error in the H37Rv reference genome. CONCLUSIONS: Our results constrain the set of genomic differences possibly affecting virulence by more than half, which focuses laboratory investigation on pertinent targets and demonstrates the power of SMRT sequencing for producing high-quality reference genomes.
[Mh] Termos MeSH primário: Mycobacterium tuberculosis/genética
Virulência/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Variações do Número de Cópias de DNA
Metilação de DNA
DNA Bacteriano/química
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
Genoma Bacteriano
Mutação
Regiões Promotoras Genéticas
Quinona Redutases/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); EC 1.6.99.- (Quinone Reductases); EC 1.6.99.5 (NADH dehydrogenase (quinone))
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1186/s12864-017-3687-5


  4 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28298441
[Au] Autor:Ito T; Murai M; Ninokura S; Kitazumi Y; Mezic KG; Cress BF; Koffas MAG; Morgan JE; Barquera B; Miyoshi H
[Ad] Endereço:From the Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan and.
[Ti] Título:Identification of the binding sites for ubiquinone and inhibitors in the Na -pumping NADH-ubiquinone oxidoreductase from by photoaffinity labeling.
[So] Source:J Biol Chem;292(19):7727-7742, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Na -pumping NADH-quinone oxidoreductase (Na -NQR) is the first enzyme of the respiratory chain and the main ion transporter in many marine and pathogenic bacteria, including The Na -NQR has been extensively studied, but its binding sites for ubiquinone and inhibitors remain controversial. Here, using a photoreactive ubiquinone PUQ-3 as well as two aurachin-type inhibitors [ I]PAD-1 and [ I]PAD-2 and photoaffinity labeling experiments on the isolated enzyme, we demonstrate that the ubiquinone ring binds to the NqrA subunit in the regions Leu-32-Met-39 and Phe-131-Lys-138, encompassing the rear wall of a predicted ubiquinone-binding cavity. The quinolone ring and alkyl side chain of aurachin bound to the NqrB subunit in the regions Arg-43-Lys-54 and Trp-23-Gly-89, respectively. These results indicate that the binding sites for ubiquinone and aurachin-type inhibitors are in close proximity but do not overlap one another. Unexpectedly, although the inhibitory effects of PAD-1 and PAD-2 were almost completely abolished by certain mutations in NqrB ( G140A and E144C), the binding reactivities of [ I]PAD-1 and [ I]PAD-2 to the mutated enzymes were unchanged compared with those of the wild-type enzyme. We also found that photoaffinity labeling by [ I]PAD-1 and [ I]PAD-2, rather than being competitively suppressed in the presence of other inhibitors, is enhanced under some experimental conditions. To explain these apparently paradoxical results, we propose models for the catalytic reaction of Na -NQR and its interactions with inhibitors on the basis of the biochemical and biophysical results reported here and in previous work.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Complexo I de Transporte de Elétrons/química
Quinona Redutases/química
Ubiquinona/química
Vibrio cholerae/enzimologia
[Mh] Termos MeSH secundário: Sítios de Ligação
Catálise
Simulação por Computador
Cristalografia por Raios X
Transporte de Elétrons
Inibidores Enzimáticos/química
Ácidos Graxos Insaturados/química
Lactonas/química
Espectrometria de Massas
Estrutura Molecular
Mutação
Marcadores de Fotoafinidade
Ligação Proteica
Pseudoalteromonas/química
Quinolonas/química
Sódio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzyme Inhibitors); 0 (Fatty Acids, Unsaturated); 0 (Lactones); 0 (Photoaffinity Labels); 0 (Quinolones); 0 (korormicin); 108354-13-8 (aurachin D); 1339-63-5 (Ubiquinone); 9NEZ333N27 (Sodium); EC 1.6.5.3 (Electron Transport Complex I); EC 1.6.99.- (Quinone Reductases); EC 1.6.99.5 (NADH dehydrogenase (quinone))
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781393


  5 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28284151
[Au] Autor:Liu W; Liu C; Liu L; You Y; Jiang J; Zhou Z; Dong Z
[Ad] Endereço:School of Life Science, The Key Laboratory of Biotechnology for Medicinal Plant of Jiangsu Province, Jiangsu Normal University, Xuzhou 221116, Jiangsu Province, China. Electronic address: leonliu2013@126.com.
[Ti] Título:Simultaneous decolorization of sulfonated azo dyes and reduction of hexavalent chromium under high salt condition by a newly isolated salt-tolerant strain Bacillus circulans BWL1061.
[So] Source:Ecotoxicol Environ Saf;141:9-16, 2017 Jul.
[Is] ISSN:1090-2414
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The co-existence of dyes, Cr(VI) and high concentration of salt in dyeing wastewater causes serious and complex environmental problems. In this study, a salt-tolerant strain Bacillus circulans BWL1061 was reported to simultaneously remove 50mg/L methyl orange and 50mg/L Cr(VI) under the anaerobic condition with 60g/L NaCl. During the decolorization process, the Cr(VI) reduction occurred preferentially over the dye decolorization due to the dominate utilization of electron by Cr(VI). The analysis of enzyme activities suggested that azoreductase, NADH-DCIP reductase, and laccase were associated with decolorization of methyl orange. A possible degradation pathway was proposed based on the metabolites analysis. The decolorization of methyl orange is involved in the symmetric cleavage of azo bond, which formed N,N-dimethyl p-phenylenediamine and 4-amino sulfonic acid, or the asymmetric cleavage of azo bond, which formed 4-(dimethylamino) phenol and 4-diazenylbenzene sulfonic acid. Phytotoxicity assays showed that strain BWL1061 could decrease the toxicity of methyl orange to Triticum aestivum, Pogostemon cablin and Isatis indigotica Fort during the decolorization process. In this study, Bacillus circulans is reported for the first time that could simultaneously remove azo dyes and Cr (VI) under high salt condition.
[Mh] Termos MeSH primário: Compostos Azo/análise
Bacillus/crescimento & desenvolvimento
Cromo/análise
Corantes/análise
Tolerância a Sal
Purificação da Água/métodos
[Mh] Termos MeSH secundário: Anaerobiose
Compostos Azo/química
Bacillus/enzimologia
Bacillus/metabolismo
Biodegradação Ambiental
Cromo/química
Corantes/química
Lacase/metabolismo
NADH NADPH Oxirredutases/metabolismo
Quinona Redutases/metabolismo
Cloreto de Sódio/metabolismo
Águas Residuais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azo Compounds); 0 (Coloring Agents); 0 (Waste Water); 0R0008Q3JB (Chromium); 18540-29-9 (chromium hexavalent ion); 451W47IQ8X (Sodium Chloride); 6B4TC34456 (methyl orange); EC 1.10.3.2 (Laccase); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.- (azoreductase); EC 1.6.99.- (Quinone Reductases); EC 1.6.99.- (dichlorophenolindophenol reductase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE


  6 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28146103
[Au] Autor:Cassagnes LE; Rakotoarivelo N; Sirigu S; Pério P; Najahi E; Chavas LM; Thompson A; Gayon R; Ferry G; Boutin JA; Valentin A; Reybier K; Nepveu F
[Ad] Endereço:UMR 152 Pharma-Dev, Université de Toulouse, IRD, UPS, 31062 Toulouse, France. laureestelle.cassagnes@gmail.com.
[Ti] Título:Role of Quinone Reductase 2 in the Antimalarial Properties of Indolone-Type Derivatives.
[So] Source:Molecules;22(2), 2017 Jan 30.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Indolone-N-oxides have antiplasmodial properties against Plasmodium falciparum at the erythrocytic stage, with IC50 values in the nanomolar range. The mechanism of action of indolone derivatives involves the production of free radicals, which follows their bioreduction by an unknown mechanism. In this study, we hypothesized that human quinone reductase 2 (hQR2), known to act as a flavin redox switch upon binding to the broadly used antimalarial chloroquine, could be involved in the activity of the redox-active indolone derivatives. Therefore, we investigated the role of hQR2 in the reduction of indolone derivatives. We analyzed the interaction between hQR2 and several indolone-type derivatives by examining enzymatic kinetics, the substrate/protein complex structure with X-ray diffraction analysis, and the production of free radicals with electron paramagnetic resonance. The reduction of each compound in cells overexpressing hQR2 was compared to its reduction in naïve cells. This process could be inhibited by the specific hQR2 inhibitor, S29434. These results confirmed that the anti-malarial activity of indolone-type derivatives was linked to their ability to serve as hQR2 substrates and not as hQR2 inhibitors as reported for chloroquine, leading to the possibility that substrate of hQR2 could be considered as a new avenue for the design of new antimalarial compounds.
[Mh] Termos MeSH primário: Antimaláricos/farmacologia
Indóis/farmacologia
Plasmodium falciparum/efeitos dos fármacos
Quinona Redutases/metabolismo
[Mh] Termos MeSH secundário: Animais
Antimaláricos/química
Células CHO
Cricetulus
Radicais Livres/metabolismo
Seres Humanos
Indóis/química
Modelos Moleculares
Estrutura Molecular
Plasmodium falciparum/metabolismo
Ligação Proteica
Conformação Proteica
Quinona Redutases/química
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimalarials); 0 (Free Radicals); 0 (Indoles); 0 (Reactive Oxygen Species); EC 1.6.99.- (Quinone Reductases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE


  7 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28142095
[Au] Autor:Paredes M; Quiles MJ
[Ad] Endereço:Departamento de Biología Vegetal, Facultad de Biología, Universidad de Murcia, Campus de Espinardo, E-30100 Murcia, Spain.
[Ti] Título:Chilling stress and hydrogen peroxide accumulation in Chrysanthemum morifolium and Spathiphyllum lanceifolium. Involvement of chlororespiration.
[So] Source:J Plant Physiol;211:36-41, 2017 Apr.
[Is] ISSN:1618-1328
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Plants of Chrysanthemum morifolium (sun species) and Spathiphyllum lanceifolium (shade species) were used to study the effects of chilling stems under high illumination. The stress conditions resulted in a greater accumulation of H O in C. morifolium than in S. lanceifolium, and in the down-regulation of photosynthetic linear electron transport in both species. However, only a slight decrease in the maximal quantum yield of PSII was observed under unfavorable conditions in both species, suggesting that mechanisms exist in the chloroplasts that dissipate excess excitation energy and prevent damage to the photosynthetic apparatus. Additionally, changes were observed in the PGR5 polypeptide involved in cyclic electron flow around PSI and in chlororespiratory enzymes (plastidial NDH complex and PTOX). The level of PGR5 increased significantly only in chilled plants of C. morifolium, whereas the levels of the PTOX and NDH-H polypeptide of the plastidial NDH complex and the NDH activity increased significantly only in chilled plants of S. lanceifolium. These findings suggest that the cyclic electron flow involving PGR5 is more active in C. morifolium, while in S. lanceifolium, other mechanisms involving chlororespiratory enzymes are stimulated in response to chilling and high light, resulting in less H O being accumulated in leaves.
[Mh] Termos MeSH primário: Araceae/metabolismo
Cloroplastos/metabolismo
Chrysanthemum/metabolismo
Temperatura Baixa
Peróxido de Hidrogênio/metabolismo
Estresse Fisiológico
[Mh] Termos MeSH secundário: Respiração Celular
Clorofila/metabolismo
Elétrons
Fluorescência
Immunoblotting
NAD/metabolismo
Peptídeos/isolamento & purificação
Peptídeos/metabolismo
Fotossíntese
Complexo de Proteína do Fotossistema II/metabolismo
Folhas de Planta/metabolismo
Plastoquinona/metabolismo
Teoria Quântica
Quinona Redutases/metabolismo
Tilacoides/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Photosystem II Protein Complex); 0U46U6E8UK (NAD); 1406-65-1 (Chlorophyll); BBX060AN9V (Hydrogen Peroxide); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); OAC30J69CN (Plastoquinone)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  8 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28107627
[Au] Autor:Augustyn KD; Jackson MR; Jorns MS
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine , Philadelphia, Pennsylvania 19102, United States.
[Ti] Título:Use of Tissue Metabolite Analysis and Enzyme Kinetics To Discriminate between Alternate Pathways for Hydrogen Sulfide Metabolism.
[So] Source:Biochemistry;56(7):986-996, 2017 Feb 21.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) is an endogenously synthesized signaling molecule that is enzymatically metabolized in mitochondria. The metabolism of H S maintains optimal concentrations of the gasotransmitter and produces sulfane sulfur (S )-containing metabolites that may be functionally important in signaling. Sulfide:quinone oxidoreductase (SQOR) catalyzes the initial two-electron oxidation of H S to S using coenzyme Q as the electron acceptor in a reaction that requires a third substrate to act as the acceptor of S . We discovered that sulfite is a highly efficient acceptor and proposed that sulfite is the physiological acceptor in a reaction that produces thiosulfate, a known metabolic intermediate. This model has been challenged by others who assume that the intracellular concentration of sulfite is very low, a scenario postulated to favor reaction of SQOR with a considerably poorer acceptor, glutathione. In this study, we measured the intracellular concentration of sulfite and other metabolites in mammalian tissues. The values observed for sulfite in rat liver (9.2 µM) and heart (38 µM) are orders of magnitude higher than previously assumed. We discovered that the apparent kinetics of oxidation of H S by SQOR with glutathione as the S acceptor reflect contributions from other SQOR-catalyzed reactions, including a novel glutathione:CoQ reductase reaction. We used observed metabolite levels and steady-state kinetic parameters to simulate rates of oxidation of H S by SQOR at physiological concentrations of different S acceptors. The results show that the reaction with sulfite as the S acceptor is a major pathway in liver and heart and provide insight into the potential dynamics of H S metabolism.
[Mh] Termos MeSH primário: Sulfeto de Hidrogênio/metabolismo
Fígado/metabolismo
Miocárdio/metabolismo
Quinona Redutases/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Animais
Cisteína/metabolismo
Glutationa/metabolismo
Cinética
Masculino
Redes e Vias Metabólicas
Quinona Redutases/química
Ratos Wistar
Sulfitos/metabolismo
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfites); 1339-63-5 (Ubiquinone); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170517
[Lr] Data última revisão:
170517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01093


  9 / 1492 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27856619
[Au] Autor:Luna-Sánchez M; Hidalgo-Gutiérrez A; Hildebrandt TM; Chaves-Serrano J; Barriocanal-Casado E; Santos-Fandila Á; Romero M; Sayed RK; Duarte J; Prokisch H; Schuelke M; Distelmaier F; Escames G; Acuña-Castroviejo D; López LC
[Ad] Endereço:Departmento de Fisiología, Facultad de Medicina, Universidad de Granada, Granada, Spain martalunasan@ugr.es luisca@ugr.es.
[Ti] Título:CoQ deficiency causes disruption of mitochondrial sulfide oxidation, a new pathomechanism associated with this syndrome.
[So] Source:EMBO Mol Med;9(1):78-95, 2017 Jan.
[Is] ISSN:1757-4684
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Coenzyme Q (CoQ) is a key component of the mitochondrial respiratory chain, but it also has several other functions in the cellular metabolism. One of them is to function as an electron carrier in the reaction catalyzed by sulfide:quinone oxidoreductase (SQR), which catalyzes the first reaction in the hydrogen sulfide oxidation pathway. Therefore, SQR may be affected by CoQ deficiency. Using human skin fibroblasts and two mouse models with primary CoQ deficiency, we demonstrate that severe CoQ deficiency causes a reduction in SQR levels and activity, which leads to an alteration of mitochondrial sulfide metabolism. In cerebrum of Coq9 mice, the deficit in SQR induces an increase in thiosulfate sulfurtransferase and sulfite oxidase, as well as modifications in the levels of thiols. As a result, biosynthetic pathways of glutamate, serotonin, and catecholamines were altered in the cerebrum, and the blood pressure was reduced. Therefore, this study reveals the reduction in SQR activity as one of the pathomechanisms associated with CoQ deficiency syndrome.
[Mh] Termos MeSH primário: Ataxia/fisiopatologia
Mitocôndrias/metabolismo
Doenças Mitocondriais/fisiopatologia
Debilidade Muscular/fisiopatologia
Quinona Redutases/metabolismo
Sulfetos/metabolismo
Ubiquinona/deficiência
[Mh] Termos MeSH secundário: Animais
Pressão Sanguínea
Células Cultivadas
Cérebro/fisiopatologia
Modelos Animais de Doenças
Fibroblastos/metabolismo
Seres Humanos
Camundongos
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfides); 1339-63-5 (Ubiquinone); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.15252/emmm.201606345


  10 / 1492 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27856618
[Au] Autor:Ziosi M; Di Meo I; Kleiner G; Gao XH; Barca E; Sanchez-Quintero MJ; Tadesse S; Jiang H; Qiao C; Rodenburg RJ; Scalais E; Schuelke M; Willard B; Hatzoglou M; Tiranti V; Quinzii CM
[Ad] Endereço:Department of Neurology, Columbia University Medical Center, New York, NY, USA.
[Ti] Título:Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway.
[So] Source:EMBO Mol Med;9(1):96-111, 2017 Jan.
[Is] ISSN:1757-4684
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Coenzyme Q (CoQ) is an electron acceptor for sulfide-quinone reductase (SQR), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and molecular abnormalities are rescued by CoQ supplementation in vitro and recapitulated by pharmacological inhibition of CoQ biosynthesis in skin fibroblasts and ADCK3 depletion in HeLa cells. Kidneys of Pdss2 mice, which only have ~15% residual CoQ concentrations and are clinically affected, showed (i) reduced protein levels of SQR and downstream enzymes, (ii) accumulation of hydrogen sulfides, and (iii) glutathione depletion. These abnormalities were not present in brain, which maintains ~30% residual CoQ and is clinically unaffected. In Pdss2 mice, we also observed low levels of plasma and urine thiosulfate and increased blood C4-C6 acylcarnitines. We propose that impairment of the sulfide oxidation pathway induced by decreased levels of CoQ causes accumulation of sulfides and consequent inhibition of short-chain acyl-CoA dehydrogenase and glutathione depletion, which contributes to increased oxidative stress and kidney failure.
[Mh] Termos MeSH primário: Ataxia/fisiopatologia
Doenças Mitocondriais/fisiopatologia
Debilidade Muscular/fisiopatologia
Sulfetos/metabolismo
Ubiquinona/deficiência
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/deficiência
Animais
Células Cultivadas
Fibroblastos/metabolismo
Seres Humanos
Camundongos
Camundongos Knockout
Oxirredução
Quinona Redutases/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfides); 1339-63-5 (Ubiquinone); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (prenyl diphosphate synthase subunit 2, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.15252/emmm.201606356



página 1 de 150 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde