Literatura científica selecionada sobre o tema "Desulfidase"
Crie uma referência precisa em APA, MLA, Chicago, Harvard, e outros estilos
Consulte a lista de atuais artigos, livros, teses, anais de congressos e outras fontes científicas relevantes para o tema "Desulfidase".
Ao lado de cada fonte na lista de referências, há um botão "Adicionar à bibliografia". Clique e geraremos automaticamente a citação bibliográfica do trabalho escolhido no estilo de citação de que você precisa: APA, MLA, Harvard, Chicago, Vancouver, etc.
Você também pode baixar o texto completo da publicação científica em formato .pdf e ler o resumo do trabalho online se estiver presente nos metadados.
Artigos de revistas sobre o assunto "Desulfidase"
Tchong, Shih-I., Huimin Xu e Robert H. White. "l-Cysteine Desulfidase: An [4Fe-4S] Enzyme Isolated fromMethanocaldococcus jannaschiiThat Catalyzes the Breakdown ofl-Cysteine into Pyruvate, Ammonia, and Sulfide†". Biochemistry 44, n.º 5 (fevereiro de 2005): 1659–70. http://dx.doi.org/10.1021/bi0484769.
Texto completo da fonteFuchs, Jonathan, Rapolas Jamontas, Maren Hellen Hoock, Jonathan Oltmanns, Béatrice Golinelli-Pimpaneau, Volker Schünemann, Antonio J. Pierik, Rolandas Meškys, Agota Aučynaitė e Matthias Boll. "TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster". Communications Biology 6, n.º 1 (27 de outubro de 2023). http://dx.doi.org/10.1038/s42003-023-05450-5.
Texto completo da fonteZhou, Yidan, e James A. Imlay. "Escherichia coli Uses a Dedicated Importer and Desulfidase To Ferment Cysteine". mBio, 4 de abril de 2022. http://dx.doi.org/10.1128/mbio.02965-21.
Texto completo da fonteGu, Huawei, Yingyin Yang, Meng Wang, Shuyi Chen, Haiying Wang, Shan Li, Yi Ma e Jufang Wang. "Novel Cysteine Desulfidase CdsB Involved in Releasing Cysteine Repression of Toxin Synthesis in Clostridium difficile". Frontiers in Cellular and Infection Microbiology 7 (9 de janeiro de 2018). http://dx.doi.org/10.3389/fcimb.2017.00531.
Texto completo da fonteNonaka, Gen, e Kazuhiro Takumi. "Cysteine degradation gene yhaM, encoding cysteine desulfidase, serves as a genetic engineering target to improve cysteine production in Escherichia coli". AMB Express 7, n.º 1 (10 de maio de 2017). http://dx.doi.org/10.1186/s13568-017-0389-y.
Texto completo da fonteLoddeke, Melissa, Barbara Schneider, Tamiko Oguri, Iti Mehta, Zhenyu Xuan e Larry Reitzer. "Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli". Journal of Bacteriology 199, n.º 16 (12 de junho de 2017). http://dx.doi.org/10.1128/jb.00117-17.
Texto completo da fonte"5449759 Hemoglobins with intersubunit desulfide bonds". Biotechnology Advances 14, n.º 4 (janeiro de 1996): 477. http://dx.doi.org/10.1016/s0734-9750(97)81627-8.
Texto completo da fonte"5449759 Hemoglobins with intersubunit desulfide bonds". Biotechnology Advances 14, n.º 4 (janeiro de 1996): 591. http://dx.doi.org/10.1016/s0734-9750(97)82040-x.
Texto completo da fonteFuchs, Jonathan, Rapolas Jamontas, Maren Hellen Hoock, Jonathan Oltmanns, Béatrice Golinelli-Pimpaneau, Volker Schünemann, Antonio J. Pierik, Rolandas Meškys, Agota Aučynaitė e Matthias Boll. "Publisher Correction: TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster". Communications Biology 6, n.º 1 (11 de dezembro de 2023). http://dx.doi.org/10.1038/s42003-023-05625-0.
Texto completo da fonteZhang, Qing, Lian Wu, Shaozheng Liu, Qingjie Chen, Lingpeng Zeng, Xuezhong Chen e Qing Zhang. "Targeted nanobody complex enhanced photodynamic therapy for lung cancer by overcoming tumor microenvironment". Cancer Cell International 20, n.º 1 (27 de novembro de 2020). http://dx.doi.org/10.1186/s12935-020-01613-0.
Texto completo da fonteTeses / dissertações sobre o assunto "Desulfidase"
Zhou, Jingjing. "Nouvelle fonction des centres [4Fe-4S] dans des réactions non-rédox : étude biochimique et structurale de thiouridylases d'ARN de transfert et d’une thiouracile désulfidase". Electronic Thesis or Diss., Sorbonne université, 2022. http://www.theses.fr/2022SORUS325.
Texto completo da fonteThe sulfur atom is an abundant and essential element for life. It is present in a wide variety of sulfur-containing biomolecules, such as certain essential amino acids - the cysteine and the methionine, which are at the center of various metabolic pathways -, transfer RNA thionucleosides, and certain essential cofactors participating in many biological processes, such as iron-sulfur centers [Fe-S]. The [Fe-S] centers are known for their redox activity and their role in electron transfer reactions. They have important cellular functions in photosynthesis, respiration, and regulation of gene translation under stress conditions. My thesis consisted of the study of two families of enzymes with [4Fe-4S] centers involved in sulfur metabolism: several transfer RNA thiouridylases (MnmA from E. coli, ThiI from archaea Methanococcus maripaludis), catalyzing sulfur insertion into tRNA uridines, as well as a ThioUracil DeSulfidase (TudS) catalyzing sulfur abstraction from thiouracil. By combining various biochemical (in vitro activity tests, site-directed mutagenesis) and biophysical (UV-visible spectroscopy, EPR, Mössbauer, X-ray crystallography) characterization methods, we were able to demonstrate the chemical nature and the role of the [4Fe-4S] cluster in the non-redox reactions catalyzed by these metalloenzymes. Identifying a reaction intermediate [4Fe-5S] in crystal, in the structure of the enzyme TudS, has confirmed a new function of the [4Fe-4S] clusters in the catalysis of non-redox reactions, previously proposed for transfer RNA thiouridylases (TtuA): the [4Fe-4S] cluster being liganded by only three amino acids, the fourth uncoordinated iron would play the role of Lewis acid by binding and activating the sulfur atom of the substrate (exogenous sulfide or thiouracil, respectively) to catalyze the reaction of thiolation (tRNA thiouridylases) or dethiolation (TudS)
Zecchin, Paolo. "Mobilisation et incorporation enzymatique du soufre lors de réactions non-redox impliquant un centre [4Fe-4S] : étude biochimique et structurale d’une cystéine désulfidase et d’une sulfurtransférase". Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS667.pdf.
Texto completo da fonteSulfur-containing compounds, such as cysteine and certain cofactors, play crucial roles in cellular processes. This thesis explores the sulfur metabolism in the anaerobic archaeum Methanococcus maripaludis, focusing on two [4Fe-4S]-dependent enzymes: L-cysteine desulfidase MmCyuA and ATP-dependent sulfur insertase MmLarE. The first part focuses on MmCyuA, which catalyzes the decomposition of L-cysteine into hydrogenosulfide and 2-aminoacrylate, subsequently converted into pyruvate and ammonia. The crystal structures of MmCyuA that we obtained, alone and in the presence of the serine inhibitor or the pyruvate product, are the first structures of a cysteine desulfidase. These structures, together with our biochemical results and spectroscopic analysis, reveal the capacity of MmCyuA to bind a [4Fe-4S] cluster, required for activity, using three or four cysteines. The structure of the enzyme in complex with serine mimics the initial step of the reaction and suggest a desulfuration mechanism for cysteine that involves the formation of a [4Fe-5S] intermediate. Comparative growth experiments between wild-type and CyuAdeficient M. maripaludis strains highlight the important role of MmCyuA for optimal growth and to enables growth using cysteine as the sole sulfur source. We propose that MmCyuA could transfer the cluster-bound sulfide to downstream acceptors, along the biosynthetic pathways of sulfurated compounds, such as [4Fe-4S]-dependent thiolation enzymes. The second part details the structure and mechanism of MmLarE. This enzyme catalyzes the sequential conversion of the two carboxylate groups of the precursor of the lactate racemase cofactor into thiocarboxylates. Two classes of LarE enzymes exist, using a sacrificial mechanism, in which a cysteine serves as the sulfur source, or a [4Fe-4S] cluster-dependent mechanism. We present the first crystal structure of a [4Fe-4S]-dependent LarE enzyme, in both its apo (without cluster) and holo (with cluster) forms. The crystal structure of holo-MmLarE reveals a [4Fe-4S] cluster coordinated by three cysteines only, with the fourth iron atom bound to an anionic ligand (chloride or phosphate group). These structures, along with our spectroscopic studies, support a mechanism in which the [4Fe-4S] cluster binds a hydrogenosulfide ligand, forming a [4Fe-5S]