Base de dados : MEDLINE
Pesquisa : D08.244.286 [Categoria DeCS]
Referências encontradas : 11175 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 1118 ir para página                         

  1 / 11175 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28660650
[Au] Autor:Zhang M; Nakanishi T; Yamanaka M; Nagao S; Yanagisawa S; Shomura Y; Shibata N; Ogura T; Higuchi Y; Hirota S
[Ad] Endereço:Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan.
[Ti] Título:Rational Design of Domain-Swapping-Based c-Type Cytochrome Heterodimers by Using Chimeric Proteins.
[So] Source:Chembiochem;18(17):1712-1715, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The design of protein oligomers with multiple active sites has been gaining interest, owing to their potential use for biomaterials, which has encouraged researchers to develop a new design method. Three-dimensional domain swapping is the unique phenomenon in which protein molecules exchange the same structural region between each other. Herein, to construct oligomeric heme proteins with different active sites by utilizing domain swapping, two c-type cytochrome-based chimeric proteins have been constructed and the domains swapped. According to X-ray crystallographic analysis, the two chimeric proteins formed a domain-swapped dimer with two His/Met coordinated hemes. By mutating the heme coordination structure of one of the two chimeric proteins, a domainswapped heterodimer with His/Met and His/H O coordinated hemes was formed. Binding of an oxygen molecule to the His/H O site of the heterodimer was confirmed by resonance Raman spectroscopy, in which the Fe-O stretching band was observed at 580 cm for the reduced/oxygenated heterodimer (at 554 cm under an O atmosphere). These results show that domain swapping is a useful method to design multiheme proteins.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
[Mh] Termos MeSH secundário: Aquifoliaceae/enzimologia
Dicroísmo Circular
Cristalografia por Raios X
Grupo dos Citocromos c/química
Grupo dos Citocromos c/genética
Dimerização
Heme/química
Heme/metabolismo
Oxigênio/química
Engenharia de Proteínas
Estrutura Terciária de Proteína
Pseudomonas aeruginosa/enzimologia
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/isolamento & purificação
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Recombinant Fusion Proteins); 42VZT0U6YR (Heme); S88TT14065 (Oxygen)
[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:170630
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700219


  2 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28388834
[Au] Autor:Haase D; Hermann B; Einsle O; Simon J
[Ad] Endereço:Microbial Energy Conversion and Biotechnology, Department of Biology, Technische Universität Darmstadt, Schnittspahnstraße 10, 64287, Darmstadt, Germany.
[Ti] Título:Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): characterization of a 'missing link' in the multihaem cytochrome c family.
[So] Source:Mol Microbiol;105(1):127-138, 2017 07.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Members of the multihaem cytochrome c family such as pentahaem cytochrome c nitrite reductase (NrfA) or octahaem hydroxylamine oxidoreductase (Hao) are involved in various microbial respiratory electron transport chains. Some members of the Hao subfamily, here called εHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Here, εHao proteins from the host-associated Epsilonproteobacteria Campylobacter fetus and Campylobacter curvus and the deep-sea hydrothermal vent bacteria Caminibacter mediatlanticus and Nautilia profundicola were purified as εHao-maltose binding protein fusions produced in Wolinella succinogenes. All four proteins were able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine whereas hydroxylamine oxidation was negligible. The introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins did neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm. In most cases, the εHao-encoding gene haoA was situated downstream of haoC, which predicts a tetrahaem cytochrome c of the NapC/NrfH family. This suggested the formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. The results indicate that εHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a 'missing link' in the evolution of NrfA and Hao enzymes.
[Mh] Termos MeSH primário: Citocromos c/metabolismo
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Grupo dos Citocromos c
Citocromos a1/metabolismo
Citocromos c1/metabolismo
Epsilonproteobacteria/genética
Epsilonproteobacteria/metabolismo
Nitrato Redutases/metabolismo
Nitritos/metabolismo
Oxirredução
Oxirredutases/genética
Wolinella/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytochrome c Group); 0 (Nitrites); 9007-43-6 (Cytochromes c); 9035-35-2 (Cytochromes a1); 9035-42-1 (Cytochromes c1); 9048-78-6 (cytochrome C-552); EC 1.- (Oxidoreductases); EC 1.7.- (Nitrate Reductases); EC 1.7.2.6 (hydroxylamine dehydrogenase); EC 1.9.6.1 (nitrate reductase (cytochrome))
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13690


  3 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28362850
[Au] Autor:Das JK; Pal Choudhury P
[Ad] Endereço:Applied Statistics Unit, Indian Statistical Institute, 203 B.T Road, Kolkata-700108, West Bengal, India.
[Ti] Título:Chemical property based sequence characterization of PpcA and its homolog proteins PpcB-E: A mathematical approach.
[So] Source:PLoS One;12(3):e0175031, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Periplasmic c7 type cytochrome A (PpcA) protein is determined in Geobacter sulfurreducens along with its other four homologs (PpcB-E). From the crystal structure viewpoint the observation emerges that PpcA protein can bind with Deoxycholate (DXCA), while its other homologs do not. But it is yet to be established with certainty the reason behind this from primary protein sequence information. This study is primarily based on primary protein sequence analysis through the chemical basis of embedded amino acids. Firstly, we look for the chemical group specific score of amino acids. Along with this, we have developed a new methodology for the phylogenetic analysis based on chemical group dissimilarities of amino acids. This new methodology is applied to the cytochrome c7 family members and pinpoint how a particular sequence is differing with others. Secondly, we build a graph theoretic model on using amino acid sequences which is also applied to the cytochrome c7 family members and some unique characteristics and their domains are highlighted. Thirdly, we search for unique patterns as subsequences which are common among the group or specific individual member. In all the cases, we are able to show some distinct features of PpcA that emerges PpcA as an outstanding protein compared to its other homologs, resulting towards its binding with deoxycholate. Similarly, some notable features for the structurally dissimilar protein PpcD compared to the other homologs are also brought out. Further, the five members of cytochrome family being homolog proteins, they must have some common significant features which are also enumerated in this study.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/classificação
Grupo dos Citocromos c/genética
Modelos Teóricos
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (cytochrome C7)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175031


  4 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28318436
[Au] Autor:Kobayashi S; Fujii S; Koga A; Wakai S; Matubayasi N; Sambongi Y
[Ad] Endereço:a Graduate School of Biosphere Science , Hiroshima University , Higashi-Hiroshima , Japan.
[Ti] Título:Pseudomonas aeruginosa cytochrome c denaturation by five systematic urea derivatives that differ in the alkyl chain length.
[So] Source:Biosci Biotechnol Biochem;81(7):1274-1278, 2017 Jul.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Reversible denaturation of Pseudomonas aeruginosa cytochrome c (PAc ) could be followed using five systematic urea derivatives that differ in the alkyl chain length, i.e. urea, N-methylurea (MU), N-ethylurea (EU), N-propylurea (PU), and N-butylurea (BU). The BU concentration was the lowest required for the PAc denaturation, those of PU, EU, MU, and urea being gradually higher. Furthermore, the accessible surface area difference upon PAc denaturation caused by BU was found to be the highest, those by PU, EU, MU, and urea being gradually lower. These findings indicate that urea derivatives with longer alkyl chains are stronger denaturants. In this study, as many as five systematic urea derivatives could be applied for the reversible denaturation of a single protein, PAc , for the first time, and the effects of the alkyl chain length on protein denaturation were systematically verified by means of thermodynamic parameters.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Grupo dos Citocromos c/química
Compostos de Metilureia/química
Pseudomonas aeruginosa/química
Ureia/análogos & derivados
Ureia/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/isolamento & purificação
Grupo dos Citocromos c/isolamento & purificação
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Compostos de Metilureia/farmacologia
Desnaturação Proteica/efeitos dos fármacos
Pseudomonas aeruginosa/enzimologia
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Relação Estrutura-Atividade
Termodinâmica
Ureia/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytochrome c Group); 0 (Methylurea Compounds); 0 (Recombinant Proteins); 0PK51J4AV7 (propylurea); 7K14B03X18 (ethylurea); 8W8T17847W (Urea); 9048-77-5 (cytochrome C(551)); 9CPL5NR15K (butylurea); VZ89YBW3P8 (methylurea)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1303361


  5 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28295618
[Au] Autor:Myung Choi J; Cao TP; Wouk Kim S; Ho Lee K; Haeng Lee S
[Ad] Endereço:Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Korea.
[Ti] Título:MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements.
[So] Source:Proteins;85(7):1379-1386, 2017 Jul.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MxaJ is a component of type II methanol dehydrogenase (MDH) that mediates electron transfer during methanol oxidation in methanotrophic bacteria. However, little is known about how MxaJ structurally cooperates with MDH and Cytochrome c . Here, we report for the first time the crystal structure of MxaJ. MxaJ consists of eight α-helices and six ß-strands, and resembles the "bi-lobate" folding architecture found in periplasmic binding proteins. Distinctive features of MxaJ include prominent loops and a ß-strand around the hinge region supporting the ligand-binding cavity, which might provide a more favorable framework for interacting with proteins rather than small molecules. Proteins 2017; 85:1379-1386. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/química
Proteínas de Bactérias/química
Grupo dos Citocromos c/química
Metanol/química
Piscirickettsiaceae/química
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Clonagem Molecular
Cristalografia por Raios X
Grupo dos Citocromos c/metabolismo
Transporte de Elétrons
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Ligantes
Metanol/metabolismo
Modelos Moleculares
Oxirredução
Piscirickettsiaceae/enzimologia
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytochrome c Group); 0 (Ligands); 0 (Recombinant Proteins); 93195-88-1 (cytochrome C(L)); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.2.8 (alcohol dehydrogenase (acceptor)); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25283


  6 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28229332
[Au] Autor:Gomaa OM; Fapetu S; Kyazze G; Keshavarz T
[Ad] Endereço:Microbiology Department, National Center for Radiation Research and Technology (NCRRT), Egyptian Atomic Energy Authority (EAEA), Cairo, Egypt. ola_gomaa@hotmail.com.
[Ti] Título:The role of riboflavin in decolourisation of Congo red and bioelectricity production using Shewanella oneidensis-MR1 under MFC and non-MFC conditions.
[So] Source:World J Microbiol Biotechnol;33(3):56, 2017 Mar.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Dissimilatory metal reducing bacteria can exchange electrons extracellularly and hold great promise for their use in simultaneous wastewater treatment and electricity production. This study investigated the role of riboflavin, an electron carrier, in the decolourisation of Congo red in microbial fuel cells (MFCs) using Shewanella oneidensis MR-1 as a model organism. The contribution of the membrane-bound protein MtrC to the decolourisation process was also investigated. Within the range of riboflavin concentrations tested, 20 µM was found to be the best with >95% of the dye (initial concentration 200 mg/L) decolourised in MFCs within 50 h compared to 90% in the case where no riboflavin was added. The corresponding maximum power density was 45 mW/m . There was no significant difference in the overall decolourisation efficiencies of Shewanela oneidensis MR-1 ΔMtrC mutants compared to the wild type. However, in terms of power production the mutant produced more power (P 76 mW/m ) compared to the wild type (P 46 mW/m ) which was attributed to higher levels of riboflavin secreted in solution. Decolourisation efficiencies in non-MFC systems (anaerobic bottles) were similar to those under MFC systems indicating that electricity generation in MFCs does not impair dye decolourisation efficiencies. The results suggest that riboflavin enhances both decolourisation of dyes and simultaneous electricity production in MFCs.
[Mh] Termos MeSH primário: Fontes de Energia Bioelétrica/microbiologia
Vermelho Congo/química
Grupo dos Citocromos c/metabolismo
Riboflavina/metabolismo
Shewanella/fisiologia
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Eletricidade
Eletrodos/microbiologia
Águas Residuais/química
Águas Residuais/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Waste Water); 3U05FHG59S (Congo Red); EC 1.- (MtrC protein, Shewanella); TLM2976OFR (Riboflavin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170224
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2223-8


  7 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28211111
[Au] Autor:Godfrey RE; Lee DJ; Busby SJW; Browning DF
[Ad] Endereço:Institute of Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
[Ti] Título:Regulation of nrf operon expression in pathogenic enteric bacteria: sequence divergence reveals new regulatory complexity.
[So] Source:Mol Microbiol;104(4):580-594, 2017 05.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Escherichia coli K-12 nrf operon encodes a periplasmic nitrite reductase, the expression of which is driven from a single promoter, pnrf. Expression from pnrf is activated by the FNR transcription factor in response to anaerobiosis and further increased in response to nitrite by the response regulator proteins, NarL and NarP. FNR-dependent transcription is suppressed by the binding of two nucleoid associated proteins, IHF and Fis. As Fis levels increase in cells grown in rich medium, the positioning of its binding site, overlapping the promoter -10 element, ensures that pnrf is sharply repressed. Here, we investigate the expression of the nrf operon promoter from various pathogenic enteric bacteria. We show that pnrf from enterohaemorrhagic E. coli is more active than its K-12 counterpart, exhibits substantial FNR-independent activity and is insensitive to nutrient quality, due to an improved -10 element. We also demonstrate that the Salmonella enterica serovar Typhimurium core promoter is more active than previously thought, due to differences around the transcription start site, and that its expression is repressed by downstream sequences. We identify the CsrA RNA binding protein as being responsible for this, and show that CsrA differentially regulates the E. coli K-12 and Salmonella nrf operons.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Nitrito Redutases/genética
Regiões Promotoras Genéticas/genética
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases/genética
Sítios de Ligação/genética
Grupo dos Citocromos c/genética
Grupo dos Citocromos c/metabolismo
Enterobacteriaceae/metabolismo
Escherichia coli/genética
Escherichia coli K12/genética
Regulação Bacteriana da Expressão Gênica/genética
Dados de Sequência Molecular
Nitrito Redutases/metabolismo
Nitritos/metabolismo
Óperon/genética
Proteínas Periplásmicas
Fatores de Transcrição/metabolismo
Sítio de Iniciação de Transcrição
Transcrição Genética/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CsrA protein, E coli); 0 (Cytochrome c Group); 0 (Escherichia coli Proteins); 0 (Nitrites); 0 (Periplasmic Proteins); 0 (RNA-Binding Proteins); 0 (Repressor Proteins); 0 (Transcription Factors); 9048-78-6 (cytochrome C-552); EC 1.7.- (Nitrite Reductases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170218
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13647


  8 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28192203
[Au] Autor:Sugimoto Y; Kitazumi Y; Shirai O; Nishikawa K; Higuchi Y; Yamamoto M; Kano K
[Ad] Endereço:Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
[Ti] Título:Electrostatic roles in electron transfer from [NiFe] hydrogenase to cytochrome c from Desulfovibrio vulgaris Miyazaki F.
[So] Source:Biochim Biophys Acta;1865(5):481-487, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Electrostatic interactions between proteins are key factors that govern the association and reaction rate. We spectroscopically determine the second-order reaction rate constant (k) of electron transfer from [NiFe] hydrogenase (H ase) to cytochrome (cyt) c at various ionic strengths (I). The k value decreases with I. To analyze the results, we develop a semi-analytical formula for I dependence of k based on the assumptions that molecules are spherical and the reaction proceeds via a transition state. Fitting of the formula to the experimental data reveals that the interaction occurs in limited regions with opposite charges and with radii much smaller than those estimated from crystal structures. This suggests that local charges in H ase and cyt c play important roles in the reaction. Although the crystallographic data indicate a positive electrostatic potential over almost the entire surface of the proteins, there exists a small region with negative potential on H ase at which the electron transfer from H ase to cyt c may occur. This local negative potential region is identical to the hypothetical interaction sphere predicted by the analysis. Furthermore, I dependence of k is predicted by the Adaptive Poisson-Boltzmann Solver considering all charges of the amino acids in the proteins and the configuration of H ase/cyt c complex. The calculation reproduces the experimental results except at extremely low I. These results indicate that the stabilization derived from the local electrostatic interaction in the H ase/cyt c complex overcomes the destabilization derived from the electrostatic repulsion of the overall positive charge of both proteins.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/química
Desulfovibrio vulgaris/enzimologia
Hidrogenase/química
Modelos Moleculares
Conformação Proteica
[Mh] Termos MeSH secundário: Respiração Celular
Grupo dos Citocromos c/metabolismo
Transporte de Elétrons
Elétrons
Hidrogenase/metabolismo
Cinética
Concentração Osmolar
Oxirredução
Mapas de Interação de Proteínas
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 9035-44-3 (cytochrome c(3)); EC 1.12.- (nickel-iron hydrogenase); EC 1.12.7.2 (Hydrogenase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE


  9 / 11175 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28141544
[Au] Autor:Refojo PN; Calisto F; Ribeiro MA; Teixeira M; Pereira MM
[Ad] Endereço:.
[Ti] Título:The monoheme cytochrome c subunit of Alternative Complex III is a direct electron donor to caa3 oxygen reductase in Rhodothermus marinus.
[So] Source:Biol Chem;398(9):1037-1044, 2017 Aug 28.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Alternative Complex III (ACIII) is an example of the robustness and flexibility of prokaryotic respiratory chains. It performs quinol:cytochrome c oxidoreductase activity, being functionally equivalent to the bc1 complex but structurally unrelated. In this work we further explored ACIII investigating the role of its monoheme cytochrome c subunit (ActE). We expressed and characterized the individually isolated ActE, which allowed us to suggest that ActE is a lipoprotein and to show its function as a direct electron donor to the caa3 oxygen reductase.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/química
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Oxirredutases/metabolismo
Subunidades Proteicas/metabolismo
Rhodothermus/enzimologia
[Mh] Termos MeSH secundário: Transporte de Elétrons
Metabolismo dos Lipídeos
Modelos Moleculares
Conformação Proteica
Subunidades Proteicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (Protein Subunits); 0 (cytochrome caa(3)); 9035-34-1 (Cytochromes a); EC 1.- (Oxidoreductases); EC 1.10.2.2 (Electron Transport Complex III)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  10 / 11175 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28054226
[Au] Autor:Zhang H; Zhai L; Wang T; Li S; Guo Y
[Ad] Endereço:Institute of Cerebrovascular Diseases, Affiliated Hospital of Qingdao University, Qingdao, 266003, China.
[Ti] Título:Picroside II Exerts a Neuroprotective Effect by Inhibiting the Mitochondria Cytochrome C Signal Pathway Following Ischemia Reperfusion Injury in Rats.
[So] Source:J Mol Neurosci;61(2):267-278, 2017 Feb.
[Is] ISSN:1559-1166
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stroke is a common neurodegenerative disease in the wide world, and mitochondrial defects underlie the pathogenesis of ischemia, especially during reperfusion. Picroside II, the principal active component of Picrorhiza, is a traditional Chinese medicine. Our previous study demonstrated that the best therapeutic dose and time window were injection of picroside II at a dose of 10-20 mg/kg body weight following cerebral ischemia by 1.5-2.0 h. In this paper, the neuroprotective effect and the mechanism of picroside II were investigated, as well as its involvement in antioxidant and mitochondria cytochrome C (CytC) signal pathway following ischemia reperfusion (I/R) injury in rats. After 24 h of cerebral I/R, the neurobehavioral function was measured by modified neurological severity score test; the content of reactive oxygen species in brain tissue was measured by enzyme-linked immunosorbent assay; the cerebral infarction volume was detected by TTC staining; the morphology of brain tissue was observed by hematoxylin-eosin; the apoptotic cells were counted by terminal deoxynucleotidyl transferase dUTP nick end labeling assay; the ultrastructure of the cortical brain tissues was observation by transmission electron microscopy; the expressions of CytC and Caspase-3 were determined by immunohistochemical assay and Western blot. The results indicated that picroside II could scavenge ROS contents, decrease the cerebral infarction volume and apoptotic cells, protect the structure of mitochondria, down-regulate the expression of CytC and Caspase-3 in cerebral I/R rats. It can be concluded that picroside II exerts a neuroprotective effect by inhibiting the mitochondria CytC signal pathway following ischemia reperfusion injury in rats.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Isquemia Encefálica/tratamento farmacológico
Cinamatos/farmacologia
Grupo dos Citocromos c/metabolismo
Glucosídeos Iridoides/farmacologia
Mitocôndrias/metabolismo
Fármacos Neuroprotetores/farmacologia
Traumatismo por Reperfusão/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Apoptose
Encéfalo/irrigação sanguínea
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Isquemia Encefálica/metabolismo
Masculino
Mitocôndrias/efeitos dos fármacos
Ratos
Ratos Wistar
Traumatismo por Reperfusão/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Cinnamates); 0 (Cytochrome c Group); 0 (Iridoid Glucosides); 0 (Neuroprotective Agents); 39012-20-9 (picroside II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1007/s12031-016-0870-0



página 1 de 1118 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