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  1 / 703 MEDLINE  
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[PMID]:28926680
[Au] Autor:Ahn JH; Bang J; Kim WJ; Lee SY
[Ad] Endereço:Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering (BK21 Plus program), BioProcess Engineering Research Center, Institute for the BioCentury, Yuseong-gu, Daejeon, Republic of Korea.
[Ti] Título:Formic acid as a secondary substrate for succinic acid production by metabolically engineered Mannheimia succiniciproducens.
[So] Source:Biotechnol Bioeng;114(12):2837-2847, 2017 Dec.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There has been much effort exerted to reduce one carbon (C1) gas emission to address climate change. As one promising way to more conveniently utilize C1 gas, several technologies have been developed to convert C1 gas into useful chemicals such as formic acid (FA). In this study, systems metabolic engineering was utilized to engineer Mannheimia succiniciproducens to efficiently utilize FA. C isotope analysis of M. succiniciproducens showed that FA could be utilized through formate dehydrogenase (FDH) reaction and/or the reverse reaction of pyruvate formate lyase (PFL). However, the naturally favored forward reaction of PFL was found to lower the SA yield from FA. In addition, FA assimilation via FDH was found to be more efficient than the reverse reaction of PFL. Thus, the M. succiniciproducens LPK7 strain, which lacks in pfl, ldh, pta, and ack genes, was selected as a base strain. In silico metabolic analysis confirmed that utilization of FA would be beneficial for the enhanced production of SA and suggested FDH as an amplification target. To find a suitable FDH, four different FDHs from M. succiniciproducens, Methylobacterium extorquens, and Candida boidinii were amplified in LPK7 strain to enhance FA assimilation. High-inoculum density cultivation using C labeled sodium formate was performed to evaluate FA assimilation efficiency. Fed-batch fermentations of the LPK7 (pMS3-fdh2 meq) strain was carried out using glucose, sucrose, or glycerol as a primary carbon source and FA as a secondary carbon source. As a result, this strain produced 76.11 g/L SA with the yield and productivity of 1.28 mol/mol and 4.08 g/L/h, respectively, using sucrose and FA as dual carbon sources. The strategy employed here will be similarly applicable in developing microorganisms to utilize FA and to produce valuable chemicals and materials from FA.
[Mh] Termos MeSH primário: Formiato Desidrogenases/genética
Formiatos/metabolismo
Melhoramento Genético/métodos
Mannheimia/fisiologia
Engenharia Metabólica/métodos
Análise do Fluxo Metabólico/métodos
Ácido Succínico/metabolismo
[Mh] Termos MeSH secundário: Simulação por Computador
Mannheimia/classificação
Modelos Biológicos
Especificidade da Espécie
Especificidade por Substrato
Ácido Succínico/isolamento & purificação
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Formates); 0YIW783RG1 (formic acid); AB6MNQ6J6L (Succinic Acid); EC 1.2.1.2 (Formate Dehydrogenases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26435


  2 / 703 MEDLINE  
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[PMID]:28784661
[Au] Autor:Yu X; Niks D; Mulchandani A; Hille R
[Ad] Endereço:From the Departments of Chemical and Environmental Engineering.
[Ti] Título:Efficient reduction of CO by the molybdenum-containing formate dehydrogenase from ( ).
[So] Source:J Biol Chem;292(41):16872-16879, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ability of the FdsABG formate dehydrogenase from (formerly known as ) to catalyze the reverse of the physiological reaction, the reduction of CO to formate utilizing NADH as electron donor, has been investigated. Contrary to previous studies of this enzyme, we demonstrate that it is in fact effective in catalyzing the reverse reaction with a of 11 ± 0.4 s We also quantify the stoichiometric accumulation of formic acid as the product of the reaction and demonstrate that the observed kinetic parameters for catalysis in the forward and reverse reactions are thermodynamically consistent, complying with the expected Haldane relationships. Finally, we demonstrate the reaction conditions necessary for gauging the ability of a given formate dehydrogenase or other CO -utilizing enzyme to catalyze the reverse direction to avoid false negative results. In conjunction with our earlier studies on the reaction mechanism of this enzyme and on the basis of the present work, we conclude that all molybdenum- and tungsten-containing formate dehydrogenases and related enzymes likely operate via a simple hydride transfer mechanism and are effective in catalyzing the reversible interconversion of CO and formate under the appropriate experimental conditions.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Dióxido de Carbono/química
Cupriavidus necator/enzimologia
Molibdênio/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Catálise
Formiato Desidrogenases
Cinética
Molibdênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 142M471B3J (Carbon Dioxide); 81AH48963U (Molybdenum); EC 1.2.1.2 (Formate Dehydrogenases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785576


  3 / 703 MEDLINE  
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[PMID]:28718449
[Au] Autor:Lindenstrauß U; Skorupa P; McDowall JS; Sargent F; Pinske C
[Ad] Endereço:Martin-Luther University Halle-Wittenberg, Institute of Biology/Microbiology, Kurt-Mothes-Str. 3, 06120 Halle, Germany.
[Ti] Título:The dual-function chaperone HycH improves assembly of the formate hydrogenlyase complex.
[So] Source:Biochem J;474(17):2937-2950, 2017 Aug 11.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The assembly of multi-protein complexes requires the concerted synthesis and maturation of its components and subsequently their co-ordinated interaction. The membrane-bound formate hydrogenlyase (FHL) complex is the primary hydrogen-producing enzyme in and is composed of seven subunits mostly encoded within the operon for [NiFe]-hydrogenase-3 (Hyd-3). The HycH protein is predicted to have an accessory function and is not part of the final structural FHL complex. In this work, a mutant strain devoid of HycH was characterised and found to have significantly reduced FHL activity due to the instability of the electron transfer subunits. HycH was shown to interact specifically with the unprocessed species of HycE, the catalytic hydrogenase subunit of the FHL complex, at different stages during the maturation and assembly of the complex. Variants of HycH were generated with the aim of identifying interacting residues and those that influence activity. The R70/71/K72, the Y79, the E81 and the Y128 variant exchanges interrupt the interaction with HycE without influencing the FHL activity. In contrast, FHL activity, but not the interaction with HycE, was negatively influenced by H37 exchanges with polar residues. Finally, a HycH Y30 variant was unstable. Surprisingly, an overlapping function between HycH with its homologous counterpart HyfJ from the operon encoding [NiFe]-hydrogenase-4 (Hyd-4) was identified and this is the first example of sharing maturation machinery components between Hyd-3 and Hyd-4 complexes. The data presented here show that HycH has a novel dual role as an assembly chaperone for a cytoplasmic [NiFe]-hydrogenase.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Formiato Desidrogenases/genética
Hidrogenase/genética
Chaperonas Moleculares/metabolismo
Complexos Multienzimáticos/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Estabilidade Enzimática/genética
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Formiato Desidrogenases/metabolismo
Hidrogenase/metabolismo
Chaperonas Moleculares/genética
Complexos Multienzimáticos/metabolismo
Mutação de Sentido Incorreto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Molecular Chaperones); 0 (Multienzyme Complexes); EC 1.12.7.2 (Hydrogenase); EC 1.2.1.2 (Formate Dehydrogenases); EC 1.2.1.2 (formate hydrogenlyase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170431


  4 / 703 MEDLINE  
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Martins, Monica
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[PMID]:28365342
[Au] Autor:Mourato C; Martins M; da Silva SM; Pereira IAC
[Ad] Endereço:Instituto de Tecnologia Química e Biológica António Xavier/Universidade Nova de Lisboa (ITQB NOVA), Av. da Republica-EAN, 2780-157 Oeiras, Portugal.
[Ti] Título:A continuous system for biocatalytic hydrogenation of CO to formate.
[So] Source:Bioresour Technol;235:149-156, 2017 Jul.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this work a novel bioprocess for hydrogenation of CO to formate was developed, using whole cell catalysis by a sulfate-reducing bacterium. Three Desulfovibrio species were tested (D. vulgaris Hildenborough, D. alaskensis G20, and D. desulfuricans ATCC 27774), of which D. desulfuricans showed the highest activity, producing 12mM of formate in batch, with a production rate of 0.09mMh . Gene expression analysis indicated that among the three formate dehydrogenases and five hydrogenases, the cytoplasmic FdhAB and the periplasmic [FeFe] HydAB are the main enzymes expressed in D. desulfuricans in these conditions. The new bioprocess for continuous formate production by D. desulfuricans had a maximum specific formate production rate of 14mMg h , and more than 45mM of formate were obtained with a production rate of 0.40mMh . This is the first report of a continuous process for biocatalytic formate production.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Formiato Desidrogenases/metabolismo
Formiatos/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Desulfovibrio/metabolismo
Hidrogenação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Formates); 142M471B3J (Carbon Dioxide); EC 1.2.1.2 (Formate Dehydrogenases)
[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:170403
[St] Status:MEDLINE


  5 / 703 MEDLINE  
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[PMID]:28201611
[Au] Autor:Takacs M; Makhlynets OV; Tolbert PL; Korendovych IV
[Ad] Endereço:Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
[Ti] Título:Secretion of functional formate dehydrogenase in Pichia pastoris.
[So] Source:Protein Eng Des Sel;30(3):381-386, 2017 Mar 01.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biofuels are an important tool for the reduction of carbon dioxide and other greenhouse emissions. NAD+-dependent formate dehydrogenase has been previously shown to be capable of the electrochemical reduction of carbon dioxide into formate, which can be ultimately converted to methanol. We established that a functional enzyme, tagged for immobilization, could be continuously secreted by Pichia pastoris. The protein can be easily separated from the growth media and its activity remains constant over an extended period of time. This is an important first step in creating a self-sustaining system capable of producing biofuels with minimal resources and space required.
[Mh] Termos MeSH primário: Formiato Desidrogenases/secreção
Proteínas Fúngicas/secreção
Pichia/enzimologia
[Mh] Termos MeSH secundário: Formiato Desidrogenases/genética
Proteínas Fúngicas/genética
Pichia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); EC 1.2.1.2 (Formate Dehydrogenases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1093/protein/gzx010


  6 / 703 MEDLINE  
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[PMID]:27887026
[Au] Autor:Aslan AS; Valjakka J; Ruupunen J; Yildirim D; Turner NJ; Turunen O; Binay B
[Ad] Endereço:Department of Chemistry, Gebze Technical University, Gebze 41400, Kocaeli, Turkey.
[Ti] Título:Chaetomium thermophilum formate dehydrogenase has high activity in the reduction of hydrogen carbonate (HCO3 -) to formate.
[So] Source:Protein Eng Des Sel;30(1):47-55, 2017 Jan.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:While formate dehydrogenases (FDHs) have been used for cofactor recycling in chemoenzymatic synthesis, the ability of FDH to reduce CO could also be utilized in the conversion of CO to useful products via formate (HCOO ). In this study, we investigated the reduction of CO in the form of hydrogen carbonate (HCO ) to formate by FDHs from Candida methylica (CmFDH) and Chaetomium thermophilum (CtFDH) in a NADH-dependent reaction. The catalytic performance with HCO as a substrate was evaluated by measuring the kinetic rates and conducting productivity assays. CtFDH showed a higher efficiency in converting HCO to formate than CmFDH, whereas CmFDH was better in the oxidation of formate. The pH optimum of the reduction was at pH 7-8. However, the high concentrations of HCO reduced the reaction rate. CtFDH was modeled in the presence of HCO showing that it fits to the active site. The active site setting for hydride transfer in CO reduction was modeled. The hydride donated by NADH would form a favorable contact to the carbon atom of HCO , resulting in a surplus of electrons within the molecule. This would cause the complex formed by hydrogen carbonate and the hydride to break into formate and hydroxide ions.
[Mh] Termos MeSH primário: Bicarbonatos/metabolismo
Chaetomium/enzimologia
Formiato Desidrogenases/metabolismo
Formiatos/metabolismo
[Mh] Termos MeSH secundário: Biotransformação
Domínio Catalítico
Formiato Desidrogenases/química
Formiato Desidrogenases/genética
Cinética
Modelos Moleculares
Oxirredução
Engenharia de Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bicarbonates); 0 (Formates); 0 (Recombinant Proteins); 0YIW783RG1 (formic acid); EC 1.2.1.2 (Formate Dehydrogenases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170503
[Lr] Data última revisão:
170503
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161126
[St] Status:MEDLINE


  7 / 703 MEDLINE  
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[PMID]:27866308
[Au] Autor:Jiang W; Xu CZ; Jiang SZ; Zhang TD; Wang SZ; Fang BS
[Ad] Endereço:Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
[Ti] Título:Establishing a Mathematical Equations and Improving the Production of L-tert-Leucine by Uniform Design and Regression Analysis.
[So] Source:Appl Biochem Biotechnol;181(4):1454-1464, 2017 Apr.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:L-tert-Leucine (L-Tle) and its derivatives are extensively used as crucial building blocks for chiral auxiliaries, pharmaceutically active ingredients, and ligands. Combining with formate dehydrogenase (FDH) for regenerating the expensive coenzyme NADH, leucine dehydrogenase (LeuDH) is continually used for synthesizing L-Tle from α-keto acid. A multilevel factorial experimental design was executed for research of this system. In this work, an efficient optimization method for improving the productivity of L-Tle was developed. And the mathematical model between different fermentation conditions and L-Tle yield was also determined in the form of the equation by using uniform design and regression analysis. The multivariate regression equation was conveniently implemented in water, with a space time yield of 505.9 g L day and an enantiomeric excess value of >99 %. These results demonstrated that this method might become an ideal protocol for industrial production of chiral compounds and unnatural amino acids such as chiral drug intermediates.
[Mh] Termos MeSH primário: Biotecnologia/métodos
Leucina/biossíntese
Modelos Teóricos
Valina/análogos & derivados
[Mh] Termos MeSH secundário: Aminação
Escherichia coli/genética
Escherichia coli/metabolismo
Formiato Desidrogenases/genética
Formiato Desidrogenases/metabolismo
Engenharia Genética
Leucina/química
Leucina Desidrogenase/genética
Leucina Desidrogenase/metabolismo
Ácido Pirúvico/química
Ácido Pirúvico/metabolismo
Análise de Regressão
Valina/biossíntese
Valina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
471-50-1 (2-amino-3,3-dimethylbutanoic acid); 8558G7RUTR (Pyruvic Acid); EC 1.2.1.2 (Formate Dehydrogenases); EC 1.4.1.9 (Leucine Dehydrogenase); GMW67QNF9C (Leucine); HG18B9YRS7 (Valine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161121
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2295-1


  8 / 703 MEDLINE  
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[PMID]:28853770
[Au] Autor:Kozhevnikova DA; Taranov EA; Lebedinsky AV; Bonch-Osmolovskaya EA; Sokolova TG
[Ti] Título:Hydrogenogenic and Sulfidogenic Growth of Thermococcus Archaea on Carbon Monoxide and Formate.
[So] Source:Mikrobiologiia;85(4):381-392, 2016 Jul.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:Enrichment and pure cultures of hyperthermophilic archaea capable of anaerobic growth on one- carbon compounds (CO and/or formate) were obtained from deep-sea sites of hydrothermal activity at the Mid-Atlantic Ridge, Lau Basin, and Guaymas Basin. All isolates belonged to the T barophilus-T paralvi- .nellae group within the genus Thermococcus. In all cases available for analysis, the genomes of Thermococcus strains capable of growth by hydrogenogenic utilization of CO and/or formate contained clusters of genes en- coding energy-converting hydrogenase and either CO dehydrogenase or formate dehydrogenase and formate transporter. Apart from the previously known processes of hydrogenogenic oxidation of CO and formate, the oxidation of these substrates coupled to sulfur reduction was observed, processes previously unknown among archaea. The capacities for hydrogenogenic or sulfidogenic oxidation of CO and formate occurred in the studied strains in all possible combinations, which could only in part be explained by peculiarities of organi- zation of genetic determinants revealed in the genomes. Investigation of CO and formate consumption kinet- ics revealed that T barophilus strain Ch5 was able to grow at concentrations close to the environmental ones. Thus, it was shown that hyperthermophilic archaea from deep-sea hydrothermal vents are able to utilize one- carbon substrates of abiotic origin both in the presence of an electron acceptor (sulfur) and in its absence. These processes were probably of importance under the conditions of the early Earth biosphere.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Monóxido de Carbono/metabolismo
Formiato Desidrogenases/metabolismo
Formiatos/metabolismo
Genoma Arqueal
Complexos Multienzimáticos/metabolismo
Thermococcus/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/genética
Oceano Atlântico
Formiato Desidrogenases/genética
Expressão Gênica
Temperatura Alta
Hidrogênio/metabolismo
Fontes Hidrotermais
Cinética
Complexos Multienzimáticos/genética
Família Multigênica
Oxirredução
Filogenia
Água do Mar
Enxofre/metabolismo
Thermococcus/classificação
Thermococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Formates); 0 (Multienzyme Complexes); 0YIW783RG1 (formic acid); 70FD1KFU70 (Sulfur); 7U1EE4V452 (Carbon Monoxide); 7YNJ3PO35Z (Hydrogen); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.2 (Formate Dehydrogenases); EC 1.2.99.2 (carbon monoxide dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170831
[St] Status:MEDLINE


  9 / 703 MEDLINE  
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[PMID]:27735784
[Au] Autor:Pinske C; Sawers RG
[Ad] Endereço:Institute of Biology/Microbiology, Martin Luther University, Halle-Wittenberg, 06120 Halle, Germany.
[Ti] Título:Anaerobic Formate and Hydrogen Metabolism.
[So] Source:EcoSal Plus;7(1), 2016 10.
[Is] ISSN:2324-6200
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Numerous recent developments in the biochemistry, molecular biology, and physiology of formate and H2 metabolism and of the [NiFe]-hydrogenase (Hyd) cofactor biosynthetic machinery are highlighted. Formate export and import by the aquaporin-like pentameric formate channel FocA is governed by interaction with pyruvate formate-lyase, the enzyme that generates formate. Formate is disproportionated by the reversible formate hydrogenlyase (FHL) complex, which has been isolated, allowing biochemical dissection of evolutionary parallels with complex I of the respiratory chain. A recently identified sulfido-ligand attached to Mo in the active site of formate dehydrogenases led to the proposal of a modified catalytic mechanism. Structural analysis of the homologous, H2-oxidizing Hyd-1 and Hyd-5 identified a novel proximal [4Fe-3S] cluster in the small subunit involved in conferring oxygen tolerance to the enzymes. Synthesis of Salmonella Typhimurium Hyd-5 occurs aerobically, which is novel for an enterobacterial Hyd. The O2-sensitive Hyd-2 enzyme has been shown to be reversible: it presumably acts as a conformational proton pump in the H2-oxidizing mode and is capable of coupling reverse electron transport to drive H2 release. The structural characterization of all the Hyp maturation proteins has given new impulse to studies on the biosynthesis of the Fe(CN)2CO moiety of the [NiFe] cofactor. It is synthesized on a Hyp-scaffold complex, mainly comprising HypC and HypD, before insertion into the apo-large subunit. Finally, clear evidence now exists indicating that Escherichia coli can mature Hyd enzymes differentially, depending on metal ion availability and the prevailing metabolic state. Notably, Hyd-3 of the FHL complex takes precedence over the H2-oxidizing enzymes.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Formiatos/metabolismo
Hidrogênio/metabolismo
Salmonella typhimurium/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Anaerobiose
Biocatálise
Transporte de Elétrons
Escherichia coli/enzimologia
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Formiato Desidrogenases/metabolismo
Hidrogenase/metabolismo
Complexos Multienzimáticos/metabolismo
Oxirredução
Salmonella typhimurium/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Formates); 0 (Multienzyme Complexes); 7YNJ3PO35Z (Hydrogen); EC 1.12.- (nickel-iron hydrogenase); EC 1.12.7.2 (Hydrogenase); EC 1.2.1.2 (Formate Dehydrogenases); EC 1.2.1.2 (formate hydrogenlyase); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.54 (formate C-acetyltransferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE
[do] DOI:10.1128/ecosalplus.ESP-0011-2016


  10 / 703 MEDLINE  
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[PMID]:27501309
[Au] Autor:Zhang L; Liu J; Ong J; Li SF
[Ad] Endereço:Department of Chemistry, Faculty of Science, National University of Singapore, Singapore 117543, Singapore.
[Ti] Título:Specific and sustainable bioelectro-reduction of carbon dioxide to formate on a novel enzymatic cathode.
[So] Source:Chemosphere;162:228-34, 2016 Nov.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To specifically convert waste CO2 into renewable chemicals, enzymatic electrosynthesis (EES) of formate from CO2 reduction was investigated in a bioelectrochemical system (BES). A novel cathode with immobilized enzyme and electropolymerized mediator-regenerator was fabricated for such bioelectrocatalytic EES. Formate dehydrogenase from Candida boidinii (CbFDH) was set as a new model enzyme in BES. Modified Nafion micelles with appropriate pore size were found to be suitable for immobilization of CbFDH and protection of its enzymatic activity and lifetime at optimal pH of 6.0. The enzymatic electrosynthesis activity of immobilized CbFDH was characterized systematically. Quite a small overpotential was required in the bioelectrochemical EES reaction. A two-electron transfer process was confirmed in the CbFDH-catalyzed reduction of bicarbonate to formate. With electro-polymerized neutral red (PolyNR) as a NADH (mediator)-regenerator, efficient formate production could be achieved at a maximum rate of 159.89 mg L(-1) h(-1) under poised potential of -0.80 V (vs. SHE). The immobilized CbFDH and electropolymerized PolyNR on an enzymatic cathode contributed greatly to sustainable EES, giving energy-rich formate as the only catalysis product.
[Mh] Termos MeSH primário: Dióxido de Carbono/química
Dióxido de Carbono/metabolismo
Eletroquímica/instrumentação
Formiato Desidrogenases/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Candida/enzimologia
Eletrodos
Transporte de Elétrons
Enzimas Imobilizadas/química
Enzimas Imobilizadas/metabolismo
Polímeros de Fluorcarboneto/química
Formiato Desidrogenases/química
Formiatos/metabolismo
Química Verde
NAD/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Fluorocarbon Polymers); 0 (Formates); 0U46U6E8UK (NAD); 0YIW783RG1 (formic acid); 142M471B3J (Carbon Dioxide); 39464-59-0 (perfluorosulfonic acid); EC 1.2.1.2 (Formate Dehydrogenases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160809
[St] Status:MEDLINE



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