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[PMID]:28919500
[Au] Autor:Mebs S; Kositzki R; Duan J; Kertess L; Senger M; Wittkamp F; Apfel UP; Happe T; Stripp ST; Winkler M; Haumann M
[Ad] Endereço:Department of Physics, Biophysics of Metalloenzymes, Freie Universität Berlin, 14195 Berlin, Germany.
[Ti] Título:Hydrogen and oxygen trapping at the H-cluster of [FeFe]-hydrogenase revealed by site-selective spectroscopy and QM/MM calculations.
[So] Source:Biochim Biophys Acta;1859(1):28-41, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:[FeFe]-hydrogenases are superior hydrogen conversion catalysts. They bind a cofactor (H-cluster) comprising a four-iron and a diiron unit with three carbon monoxide (CO) and two cyanide (CN ) ligands. Hydrogen (H ) and oxygen (O ) binding at the H-cluster was studied in the C169A variant of [FeFe]-hydrogenase HYDA1, in comparison to the active oxidized (Hox) and CO-inhibited (Hox-CO) species in wildtype enzyme. Fe labeling of the diiron site was achieved by in vitro maturation with a synthetic cofactor analogue. Site-selective X-ray absorption, emission, and nuclear inelastic/forward scattering methods and infrared spectroscopy were combined with quantum chemical calculations to determine the molecular and electronic structure and vibrational dynamics of detected cofactor species. Hox reveals an apical vacancy at Fe in a [4Fe4S-2Fe] complex with the net spin on Fe whereas Hox-CO shows an apical CN at Fe in a [4Fe4S-2Fe(CO)] complex with net spin sharing among Fe and Fe (proximal or distal iron ions in [2Fe]). At ambient O pressure, a novel H-cluster species (Hox-O ) accumulated in C169A, assigned to a [4Fe4S-2Fe(O )] complex with an apical superoxide (O ) carrying the net spin bound at Fe . H exposure populated the two-electron reduced Hhyd species in C169A, assigned as a [(H)4Fe4S-2Fe(H)] complex with the net spin on the reduced cubane, an apical hydride at Fe , and a proton at a cysteine ligand. Hox-O and Hhyd are stabilized by impaired O protonation or proton release after H cleavage due to interruption of the proton path towards and out of the active site.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/enzimologia
Hidrogênio/química
Hidrogenase/química
Proteínas com Ferro-Enxofre/química
Oxigênio/química
Proteínas de Plantas/química
[Mh] Termos MeSH secundário: Domínio Catalítico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Plant Proteins); 7YNJ3PO35Z (Hydrogen); EC 1.12.7.2 (Hydrogenase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


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[PMID]:28470848
[Au] Autor:Camprubi E; Jordan SF; Vasiliadou R; Lane N
[Ad] Endereço:Department of Genetics, Evolution and Environment, University College London, London, UK.
[Ti] Título:Iron catalysis at the origin of life.
[So] Source:IUBMB Life;69(6):373-381, 2017 06.
[Is] ISSN:1521-6551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Iron-sulphur proteins are ancient and drive fundamental processes in cells, notably electron transfer and CO fixation. Iron-sulphur minerals with equivalent structures could have played a key role in the origin of life. However, the 'iron-sulphur world' hypothesis has had a mixed reception, with questions raised especially about the feasibility of a pyrites-pulled reverse Krebs cycle. Phylogenetics suggests that the earliest cells drove carbon and energy metabolism via the acetyl CoA pathway, which is also replete in Fe(Ni)S proteins. Deep differences between bacteria and archaea in this pathway obscure the ancestral state. These differences make sense if early cells depended on natural proton gradients in alkaline hydrothermal vents. If so, the acetyl CoA pathway diverged with the origins of active ion pumping, and ancestral CO fixation might have been equivalent to methanogens, which depend on a membrane-bound NiFe hydrogenase, energy converting hydrogenase. This uses the proton-motive force to reduce ferredoxin, thence CO . The mechanism suggests that pH could modulate reduction potential at the active site of the enzyme, facilitating the difficult reduction of CO by H . This mechanism could be generalised under abiotic conditions so that steep pH differences across semi-conducting Fe(Ni)S barriers drives not just the first steps of CO fixation to C1 and C2 organics such as CO, CH SH and CH COSH, but a series of similar carbonylation and hydrogenation reactions to form longer chain carboxylic acids such as pyruvate, oxaloacetate and α-ketoglutarate, as in the incomplete reverse Krebs cycle found in methanogens. We suggest that the closure of a complete reverse Krebs cycle, by regenerating acetyl CoA directly, displaced the acetyl CoA pathway from many modern groups. A later reliance on acetyl CoA and ATP eliminated the need for the proton-motive force to drive most steps of the reverse Krebs cycle. © 2017 IUBMB Life, 69(6):373-381, 2017.
[Mh] Termos MeSH primário: Acetilcoenzima A/química
Ferredoxinas/química
Proteínas com Ferro-Enxofre/química
Ferro/química
Origem da Vida
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Archaea/química
Archaea/metabolismo
Bactérias/química
Bactérias/metabolismo
Ciclo do Carbono
Dióxido de Carbono/química
Dióxido de Carbono/metabolismo
Catálise
Ciclo do Ácido Cítrico
Ferredoxinas/metabolismo
Concentração de Íons de Hidrogênio
Fontes Hidrotermais
Ferro/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Ácidos Cetoglutáricos/química
Ácidos Cetoglutáricos/metabolismo
Ácido Oxaloacético/química
Ácido Oxaloacético/metabolismo
Prótons
Ácido Pirúvico/química
Ácido Pirúvico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ferredoxins); 0 (Iron-Sulfur Proteins); 0 (Ketoglutaric Acids); 0 (Protons); 142M471B3J (Carbon Dioxide); 2F399MM81J (Oxaloacetic Acid); 72-89-9 (Acetyl Coenzyme A); 8558G7RUTR (Pyruvic Acid); 8ID597Z82X (alpha-ketoglutaric acid); E1UOL152H7 (Iron)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1002/iub.1632


  3 / 4851 MEDLINE  
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[PMID]:29188999
[Au] Autor:Song LC; Zhu L; Hu FQ; Wang YX
[Ad] Endereço:Department of Chemistry, State Key Laboratory of Elemento-Organic Chemistry, College of Chemistry, and ‡Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Nankai University , Tianjin 300071, China.
[Ti] Título:Studies on Chemical Reactivity and Electrocatalysis of Two Acylmethyl(hydroxymethyl)pyridine Ligand-Containing [Fe]-Hydrogenase Models (2-COCH -6-HOCH C H N)Fe(CO) L (L = η -SCOMe, η -2-SC H N).
[So] Source:Inorg Chem;56(24):15216-15230, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:On the basis of preparation and characterization of [Fe]-H ase models (2-COCH -6-HOCH C H N)Fe(CO) L (A, L = η -SCOMe; B, L = η -2-SC H N), the chemical reactivities of A and B with various electrophilic and nucleophilic reagents have been investigated, systematically. Thus, when A reacted with 1 equiv of MeCOCl in the presence of Et N in MeCN to give the η -SCOMe-coordinated acylation product (2-COCH -6-MeCO CH C H N)Fe(CO) (η -SCOMe) (1), treatment of A with excess HBF ·Et O in MeCN gave the cationic MeCN-coordinated complex [(2-COCH -6-HOCH C H N)Fe(CO) (MeCN)](BF ) (2). In addition, when 2 was treated with 1 equiv of 2,6-(p-4-MeC H ) C H SK or PPh in CH Cl to give the thiophenolato- and PPh -substituted derivatives (2-COCH -6-HOCH C H N)Fe(CO) [2,6-(p-MeC H ) C H S] (3) and [(2-COCH -6-HOCH C H N)Fe(CO) (PPh )](BF ) (4), treatment of B with 1 equiv of PMe or P(OMe) in THF afforded the phosphine- and phosphite-substituted complexes (2-COCH -6-HOCH C H N)(η -2-SC H N)Fe(CO) L (5, L = PMe ; 6, L = P(OMe) ). Interestingly, in contrast to A, when B reacted with excess HBF ·Et O in MeCN to afford the BF adduct [2-COCH -6-HO(BF )CH C H N]Fe(CO) (η -2-SC H N) (7), reaction of B with 1 equiv of p-MeC H COCl in the presence of Et N in MeCN gave not only the expected 2-acylmethyl-6-p-toluoyloxomethylpyridine-containing complex (2-COCH -6-p-MeC H CO CH C H N)Fe(CO) (η -2-SC H N) (8), but also gave the unexpected 2-toluoyloxovinyl-6-toluoyloxomethylpyridine-containing complex (2-p-MeC H CO C H-6-p-MeC H CO CH C H N)Fe(CO) (η -2-SC H N) (9). While the possible pathways for the novel reactions leading to complexes 1, 2, and 7-9 are suggested, the structures of complexes B, 1-4, and 6-9 were unambiguously confirmed by X-ray crystallography. In addition, model complexes A and B have been found to be catalysts for proton reduction to H from TFA under CV conditions.
[Mh] Termos MeSH primário: Materiais Biomiméticos/química
Hidrogenase/química
Compostos de Ferro/química
Proteínas com Ferro-Enxofre/química
Piridinas/química
[Mh] Termos MeSH secundário: Catálise
Cristalografia por Raios X
Técnicas Eletroquímicas
Ligantes
Modelos Moleculares
Oxirredução
Prótons
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron Compounds); 0 (Iron-Sulfur Proteins); 0 (Ligands); 0 (Protons); 0 (Pyridines); 0 (acylmethyl(hydroxymethyl)pyridine); EC 1.12.- (iron hydrogenase); EC 1.12.7.2 (Hydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b02582


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[PMID]:27773628
[Au] Autor:Choby JE; Mike LA; Mashruwala AA; Dutter BF; Dunman PM; Sulikowski GA; Boyd JM; Skaar EP
[Ad] Endereço:Department of Pathology, Microbiology, & Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Graduate Program in Microbiology & Immunology, Vanderbilt University, Nashville, TN 37232, USA.
[Ti] Título:A Small-Molecule Inhibitor of Iron-Sulfur Cluster Assembly Uncovers a Link between Virulence Regulation and Metabolism in Staphylococcus aureus.
[So] Source:Cell Chem Biol;23(11):1351-1361, 2016 Nov 17.
[Is] ISSN:2451-9448
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The rising problem of antimicrobial resistance in Staphylococcus aureus necessitates the discovery of novel therapeutic targets for small-molecule intervention. A major obstacle of drug discovery is identifying the target of molecules selected from high-throughput phenotypic assays. Here, we show that the toxicity of a small molecule termed '882 is dependent on the constitutive activity of the S. aureus virulence regulator SaeRS, uncovering a link between virulence factor production and energy generation. A series of genetic, physiological, and biochemical analyses reveal that '882 inhibits iron-sulfur (Fe-S) cluster assembly most likely through inhibition of the Suf complex, which synthesizes Fe-S clusters. In support of this, '882 supplementation results in decreased activity of the Fe-S cluster-dependent enzyme aconitase. Further information regarding the effects of '882 has deepened our understanding of virulence regulation and demonstrates the potential for small-molecule modulation of Fe-S cluster assembly in S. aureus and other pathogens.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Bibliotecas de Moléculas Pequenas/farmacologia
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Antibacterianos/química
Descoberta de Drogas
Seres Humanos
Proteínas Quinases/metabolismo
Transdução de Sinais/efeitos dos fármacos
Bibliotecas de Moléculas Pequenas/química
Infecções Estafilocócicas/microbiologia
Staphylococcus aureus/crescimento & desenvolvimento
Staphylococcus aureus/metabolismo
Fatores de Transcrição/metabolismo
Virulência/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Iron-Sulfur Proteins); 0 (SaeR protein, Staphylococcus aureus); 0 (Small Molecule Libraries); 0 (Transcription Factors); 0 (Virulence Factors); EC 2.7.- (Protein Kinases); EC 2.7.3.- (SaeS protein, Staphylococcus aureus); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:29223152
[Au] Autor:Cherepanov DA; Milanovsky GE; Petrova AA; Tikhonov AN; Semenov AY
[Ad] Endereço:Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, Moscow, 119992, Russia. tscherepanov@gmail.com.
[Ti] Título:Electron Transfer through the Acceptor Side of Photosystem I: Interaction with Exogenous Acceptors and Molecular Oxygen.
[So] Source:Biochemistry (Mosc);82(11):1249-1268, 2017 Nov.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This review considers the state-of-the-art on mechanisms and alternative pathways of electron transfer in photosynthetic electron transport chains of chloroplasts and cyanobacteria. The mechanisms of electron transport control between photosystems (PS) I and II and the Calvin-Benson cycle are considered. The redistribution of electron fluxes between the noncyclic, cyclic, and pseudocyclic pathways plays an important role in the regulation of photosynthesis. Mathematical modeling of light-induced electron transport processes is considered. Particular attention is given to the electron transfer reactions on the acceptor side of PS I and to interactions of PS I with exogenous acceptors, including molecular oxygen. A kinetic model of PS I and its interaction with exogenous electron acceptors has been developed. This model is based on experimental kinetics of charge recombination in isolated PS I. Kinetic and thermodynamic parameters of the electron transfer reactions in PS I are scrutinized. The free energies of electron transfer between quinone acceptors A /A in the symmetric redox cofactor branches of PS I and iron-sulfur clusters F , F , and F have been estimated. The second-order rate constants of electron transfer from PS I to external acceptors have been determined. The data suggest that byproduct formation of superoxide radical in PS I due to the reduction of molecular oxygen in the A site (Mehler reaction) can exceed 0.3% of the total electron flux in PS I.
[Mh] Termos MeSH primário: Transporte de Elétrons
Complexo de Proteína do Fotossistema I/metabolismo
[Mh] Termos MeSH secundário: Cloroplastos/química
Cloroplastos/metabolismo
Cianobactérias/química
Cianobactérias/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Cinética
Modelos Químicos
Oxigênio/metabolismo
Quinonas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Photosystem I Protein Complex); 0 (Quinones); S88TT14065 (Oxygen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917110037


  6 / 4851 MEDLINE  
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[PMID]:28965846
[Au] Autor:Paul A; Drecourt A; Petit F; Deguine DD; Vasnier C; Oufadem M; Masson C; Bonnet C; Masmoudi S; Mosnier I; Mahieu L; Bouccara D; Kaplan J; Challe G; Domange C; Mochel F; Sterkers O; Gerber S; Nitschke P; Bole-Feysot C; Jonard L; Gherbi S; Mercati O; Ben Aissa I; Lyonnet S; Rötig A; Delahodde A; Marlin S
[Ad] Endereço:UMR 1163, Université Paris Descartes, Sorbonne Paris Cité, Institut IMAGINE, 24 Boulevard du Montparnasse, 75015 Paris, France.
[Ti] Título:FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of Mitochondrial Fe-S-Synthesis Diseases.
[So] Source:Am J Hum Genet;101(4):630-637, 2017 Oct 05.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hearing loss and visual impairment in childhood have mostly genetic origins, some of them being related to sensorial neuronal defects. Here, we report on eight subjects from four independent families affected by auditory neuropathy and optic atrophy. Whole-exome sequencing revealed biallelic mutations in FDXR in affected subjects of each family. FDXR encodes the mitochondrial ferredoxin reductase, the sole human ferredoxin reductase implicated in the biosynthesis of iron-sulfur clusters (ISCs) and in heme formation. ISC proteins are involved in enzymatic catalysis, gene expression, and DNA replication and repair. We observed deregulated iron homeostasis in FDXR mutant fibroblasts and indirect evidence of mitochondrial iron overload. Functional complementation in a yeast strain in which ARH1, the human FDXR ortholog, was deleted established the pathogenicity of these mutations. These data highlight the wide clinical heterogeneity of mitochondrial disorders related to ISC synthesis.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/genética
Perda Auditiva Central/genética
Proteínas com Ferro-Enxofre/metabolismo
Ferro/metabolismo
Doenças Mitocondriais/genética
Mutação
Atrofia Óptica/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Sequência de Aminoácidos
Pré-Escolar
Feminino
Ferredoxina-NADP Redutase/química
Ferredoxina-NADP Redutase/metabolismo
Teste de Complementação Genética
Perda Auditiva Central/enzimologia
Perda Auditiva Central/patologia
Seres Humanos
Proteínas com Ferro-Enxofre/genética
Masculino
Mitocôndrias/enzimologia
Mitocôndrias/genética
Mitocôndrias/patologia
Doenças Mitocondriais/enzimologia
Doenças Mitocondriais/patologia
Atrofia Óptica/enzimologia
Atrofia Óptica/patologia
Linhagem
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Saccharomyces cerevisiae Proteins); E1UOL152H7 (Iron); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE


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[PMID]:28949132
[Au] Autor:Goetzl S; Teutloff C; Werther T; Hennig SE; Jeoung JH; Bittl R; Dobbek H
[Ad] Endereço:Institut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin , Berlin, Germany.
[Ti] Título:Protein Dynamics in the Reductive Activation of a B12-Containing Enzyme.
[So] Source:Biochemistry;56(41):5496-5502, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:B12-dependent proteins are involved in methyl transfer reactions ranging from the biosynthesis of methionine in humans to the formation of acetyl-CoA in anaerobic bacteria. During their catalytic cycle, they undergo large conformational changes to interact with various proteins. Recently, the crystal structure of the B12-containing corrinoid iron-sulfur protein (CoFeSP) in complex with its reductive activator (RACo) was determined, providing a first glimpse of how energy is transduced in the ATP-dependent reductive activation of corrinoid-containing methyltransferases. The thermodynamically uphill electron transfer from RACo to CoFeSP is accompanied by large movements of the cofactor-binding domains of CoFeSP. To refine the structure-based mechanism, we analyzed the conformational change of the B12-binding domain of CoFeSP by pulsed electron-electron double resonance and Förster resonance energy transfer spectroscopy. We show that the site-specific labels on the flexible B12-binding domain and the small subunit of CoFeSP move within 11 Å in the RACo:CoFeSP complex, consistent with the recent crystal structures. By analyzing the transient kinetics of formation and dissociation of the RACo:CoFeSP complex, we determined values of 0.75 µM s and 0.33 s for rate constants k and k , respectively. Our results indicate that the large movement observed in crystals also occurs in solution and that neither the formation of the protein encounter complex nor the large movement of the B12-binding domain is rate-limiting for the ATP-dependent reductive activation of CoFeSP by RACo.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Coenzimas/metabolismo
Ativadores de Enzimas/metabolismo
Firmicutes/enzimologia
Proteínas com Ferro-Enxofre/metabolismo
Modelos Moleculares
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/química
Aldeído Oxirredutases/genética
Aldeído Oxirredutases/metabolismo
Substituição de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Coenzimas/química
Cristalografia por Raios X
Bases de Dados de Proteínas
Dimerização
Ativadores de Enzimas/química
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Cinética
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Oxirredução
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Vitamina B 12/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Enzyme Activators); 0 (Iron-Sulfur Proteins); 0 (Multienzyme Complexes); 0 (Protein Subunits); 0 (Recombinant Proteins); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.99.2 (carbon monoxide dehydrogenase); P6YC3EG204 (Vitamin B 12)
[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:170927
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00477


  8 / 4851 MEDLINE  
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[PMID]:28847921
[Au] Autor:Jiang T; Guo X; Yan J; Zhang Y; Wang Y; Zhang M; Sheng B; Ma C; Xu P; Gao C
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
[Ti] Título:A Bacterial Multidomain NAD-Independent d-Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d-Lactate Oxidization.
[So] Source:J Bacteriol;199(22), 2017 Nov 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial membrane-associated NAD-independent d-lactate dehydrogenase (Fe-S d-iLDH) oxidizes d-lactate into pyruvate. A sequence analysis of the enzyme reveals that it contains an Fe-S oxidoreductase domain in addition to a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain, which differs from other typical d-iLDHs. Fe-S d-iLDH from KT2440 was purified as a His-tagged protein and characterized in detail. This monomeric enzyme exhibited activities with l-lactate and several d-2-hydroxyacids. Quinone was shown to be the preferred electron acceptor of the enzyme. The two domains of the enzyme were then heterologously expressed and purified separately. The Fe-S cluster-binding motifs predicted by sequence alignment were preliminarily verified by site-directed mutagenesis of the Fe-S oxidoreductase domain. The FAD-containing dehydrogenase domain retained 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S d-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain showed increased catalytic efficiency with cytochrome as the electron acceptor, but it completely lost the ability to use coenzyme Q Additionally, the FAD-containing dehydrogenase domain was no longer associated with the cell membrane, and it could not support the utilization of d-lactate as a carbon source. Based on the results obtained, we conclude that the Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S d-iLDH, and it helps the enzyme associate with the cell membrane. These functions make the Fe-S oxidoreductase domain crucial for the d-lactate utilization function of Fe-S d-iLDH. Lactate metabolism plays versatile roles in most domains of life. Lactate utilization processes depend on certain enzymes to oxidize lactate to pyruvate. In recent years, novel bacterial lactate-oxidizing enzymes have been continually reported, including the unique NAD-independent d-lactate dehydrogenase that contains an Fe-S oxidoreductase domain besides the typical flavin-containing domain (Fe-S d-iLDH). Although Fe-S d-iLDH is widely distributed among bacterial species, the investigation of it is insufficient. Fe-S d-iLDH from KT2440, which is the major d-lactate-oxidizing enzyme for the strain, might be a representative of this type of enzyme. A study of it will be helpful in understanding the detailed mechanisms underlying the lactate utilization processes.
[Mh] Termos MeSH primário: Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Lactato Desidrogenases/genética
Lactato Desidrogenases/metabolismo
Ácido Láctico/metabolismo
Quinonas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Coenzimas
Citocromos c/metabolismo
Elétrons
Lactato Desidrogenases/isolamento & purificação
Mutagênese Sítio-Dirigida
NAD/metabolismo
Oxirredução
Pseudomonas putida/enzimologia
Ubiquinona/análogos & derivados
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Iron-Sulfur Proteins); 0 (Quinones); 0U46U6E8UK (NAD); 1339-63-5 (Ubiquinone); 146-14-5 (Flavin-Adenine Dinucleotide); 33X04XA5AT (Lactic Acid); 9007-43-6 (Cytochromes c); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.1.28 (D-lactate dehydrogenase); EJ27X76M46 (coenzyme Q10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE


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[PMID]:28830931
[Au] Autor:Latham JA; Barr I; Klinman JP
[Ad] Endereço:From the Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado 80208 and.
[Ti] Título:At the confluence of ribosomally synthesized peptide modification and radical -adenosylmethionine (SAM) enzymology.
[So] Source:J Biol Chem;292(40):16397-16405, 2017 Oct 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Radical -adenosylmethionine (RS) enzymology has emerged as a major biochemical strategy for the homolytic cleavage of unactivated C-H bonds. At the same time, the post-translational modification of ribosomally synthesized peptides is a rapidly expanding area of investigation. We discuss the functional cross-section of these two disciplines, highlighting the recently uncovered importance of protein-protein interactions, especially between the peptide substrate and its chaperone, which functions either as a stand-alone protein or as an N-terminal fusion to the respective enzyme. The need for further work on this class of enzymes is emphasized, given the poorly understood roles performed by multiple, auxiliary iron-sulfur clusters and the paucity of protein X-ray structural data.
[Mh] Termos MeSH primário: Proteínas com Ferro-Enxofre
Chaperonas Moleculares
Processamento de Proteína Pós-Traducional/fisiologia
S-Adenosilmetionina
[Mh] Termos MeSH secundário: Radicais Livres/química
Radicais Livres/metabolismo
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/metabolismo
Chaperonas Moleculares/química
Chaperonas Moleculares/metabolismo
S-Adenosilmetionina/química
S-Adenosilmetionina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Free Radicals); 0 (Iron-Sulfur Proteins); 0 (Molecular Chaperones); 7LP2MPO46S (S-Adenosylmethionine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.797399


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[PMID]:28821607
[Au] Autor:Tripathi SK; Xu T; Feng Q; Avula B; Shi X; Pan X; Mask MM; Baerson SR; Jacob MR; Ravu RR; Khan SI; Li XC; Khan IA; Clark AM; Agarwal AK
[Ad] Endereço:From the National Center for Natural Products Research.
[Ti] Título:Two plant-derived aporphinoid alkaloids exert their antifungal activity by disrupting mitochondrial iron-sulfur cluster biosynthesis.
[So] Source:J Biol Chem;292(40):16578-16593, 2017 Oct 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eupolauridine and liriodenine are plant-derived aporphinoid alkaloids that exhibit potent inhibitory activity against the opportunistic fungal pathogens and However, the molecular mechanism of this antifungal activity is unknown. In this study, we show that eupolauridine 9591 (E9591), a synthetic analog of eupolauridine, and liriodenine methiodide (LMT), a methiodide salt of liriodenine, mediate their antifungal activities by disrupting mitochondrial iron-sulfur (Fe-S) cluster synthesis. Several lines of evidence supported this conclusion. First, both E9591 and LMT elicited a transcriptional response indicative of iron imbalance, causing the induction of genes that are required for iron uptake and for the maintenance of cellular iron homeostasis. Second, a genome-wide fitness profile analysis showed that yeast mutants with deletions in iron homeostasis-related genes were hypersensitive to E9591 and LMT. Third, treatment of wild-type yeast cells with E9591 or LMT generated cellular defects that mimicked deficiencies in mitochondrial Fe-S cluster synthesis including an increase in mitochondrial iron levels, a decrease in the activities of Fe-S cluster enzymes, a decrease in respiratory function, and an increase in oxidative stress. Collectively, our results demonstrate that E9591 and LMT perturb mitochondrial Fe-S cluster biosynthesis; thus, these two compounds target a cellular pathway that is distinct from the pathways commonly targeted by clinically used antifungal drugs. Therefore, the identification of this pathway as a target for antifungal compounds has potential applications in the development of new antifungal therapies.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Aporfinas/farmacologia
Candida albicans
Proteínas Fúngicas
Indenos/farmacologia
Proteínas com Ferro-Enxofre
Proteínas Mitocondriais
Naftiridinas/farmacologia
[Mh] Termos MeSH secundário: Antifúngicos/química
Aporfinas/química
Candida albicans/genética
Candida albicans/crescimento & desenvolvimento
Cryptococcus neoformans/genética
Cryptococcus neoformans/crescimento & desenvolvimento
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Estudo de Associação Genômica Ampla
Indenos/química
Proteínas com Ferro-Enxofre/genética
Proteínas com Ferro-Enxofre/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Naftiridinas/química
Estresse Oxidativo/efeitos dos fármacos
Estresse Oxidativo/genética
Consumo de Oxigênio/efeitos dos fármacos
Consumo de Oxigênio/genética
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Aporphines); 0 (Fungal Proteins); 0 (Indenes); 0 (Iron-Sulfur Proteins); 0 (Mitochondrial Proteins); 0 (Naphthyridines); 58786-39-3 (eupolauridine); E134R7X4O9 (liriodenine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781773



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