Literatura científica selecionada sobre o tema "Sulfur insertase"
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 "Sulfur insertase".
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 "Sulfur insertase"
Fellner, Matthias, Benoît Desguin, Robert P. Hausinger e Jian Hu. "Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE". Proceedings of the National Academy of Sciences 114, n.º 34 (7 de agosto de 2017): 9074–79. http://dx.doi.org/10.1073/pnas.1704967114.
Texto completo da fonteFellner, Matthias, Joel A. Rankin, Benoît Desguin, Jian Hu e Robert P. Hausinger. "Analysis of the Active Site Cysteine Residue of the Sacrificial Sulfur Insertase LarE from Lactobacillus plantarum". Biochemistry 57, n.º 38 (29 de agosto de 2018): 5513–23. http://dx.doi.org/10.1021/acs.biochem.8b00601.
Texto completo da fonteLeimkühler, Silke, e Werner Klipp. "Role of XDHC in Molybdenum Cofactor Insertion into Xanthine Dehydrogenase of Rhodobacter capsulatus". Journal of Bacteriology 181, n.º 9 (1 de maio de 1999): 2745–51. http://dx.doi.org/10.1128/jb.181.9.2745-2751.1999.
Texto completo da fonteWunsch, Patrick, Margitta Herb, Hagen Wieland, Ulrike M. Schiek e Walter G. Zumft. "Requirements for CuA and Cu-S Center Assembly of Nitrous Oxide Reductase Deduced from Complete Periplasmic Enzyme Maturation in the Nondenitrifier Pseudomonas putida". Journal of Bacteriology 185, n.º 3 (1 de fevereiro de 2003): 887–96. http://dx.doi.org/10.1128/jb.185.3.887-896.2003.
Texto completo da fonteRudenko, Tatyana S., Sergey V. Tarlachkov, Nikolay D. Shatskiy e Margarita Yu Grabovich. "Comparative Genomics of Beggiatoa leptomitoformis Strains D-401 and D-402T with Contrasting Physiology But Extremely High Level of Genomic Identity". Microorganisms 8, n.º 6 (19 de junho de 2020): 928. http://dx.doi.org/10.3390/microorganisms8060928.
Texto completo da fonteYe, Ke-Yin, Markus Bursch, Zheng-Wang Qu, Constantin G. Daniliuc, Stefan Grimme, Gerald Kehr e Gerhard Erker. "Reversible formylborane/SO2coupling at a frustrated Lewis pair framework". Chemical Communications 53, n.º 3 (2017): 633–35. http://dx.doi.org/10.1039/c6cc07071j.
Texto completo da fontePaietta, J. V., R. A. Akins, A. M. Lambowitz e G. A. Marzluf. "Molecular cloning and characterization of the cys-3 regulatory gene of Neurospora crassa." Molecular and Cellular Biology 7, n.º 7 (julho de 1987): 2506–11. http://dx.doi.org/10.1128/mcb.7.7.2506.
Texto completo da fonteTimina, Olga, Oleg Timin e Anna Stepanova. "Some biochemical characteristics of the hairy roots of Pisum sativum L. mutants". Ecological genetics 21, n.º 3S (4 de dezembro de 2023): 40. http://dx.doi.org/10.17816/ecogen568310.
Texto completo da fontePinto, Rachel, Joseph S. Harrison, Tsungda Hsu, William R. Jacobs e Thomas S. Leyh. "Sulfite Reduction in Mycobacteria". Journal of Bacteriology 189, n.º 18 (20 de julho de 2007): 6714–22. http://dx.doi.org/10.1128/jb.00487-07.
Texto completo da fonteDouglas, Paul, Marco Kriek, Penny Bryant e Peter L. Roach. "Lipoyl Synthase Inserts Sulfur Atoms into an Octanoyl Substrate in a Stepwise Manner". Angewandte Chemie 118, n.º 31 (4 de agosto de 2006): 5321–23. http://dx.doi.org/10.1002/ange.200601910.
Texto completo da fonteTeses / dissertações sobre o assunto "Sulfur insertase"
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]