Artículos de revistas sobre el tema "Structural Modeling - Heme Enzymes"
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Jóźwik, Ilona K., Martin Litzenburger, Yogan Khatri, Alexander Schifrin, Marco Girhard, Vlada Urlacher, Andy-Mark W. H. Thunnissen y Rita Bernhardt. "Structural insights into oxidation of medium-chain fatty acids and flavanone by myxobacterial cytochrome P450 CYP267B1". Biochemical Journal 475, n.º 17 (11 de septiembre de 2018): 2801–17. http://dx.doi.org/10.1042/bcj20180402.
Texto completoRobins, Tiina, Jonas Carlsson, Maria Sunnerhagen, Anna Wedell y Bengt Persson. "Molecular Model of Human CYP21 Based on Mammalian CYP2C5: Structural Features Correlate with Clinical Severity of Mutations Causing Congenital Adrenal Hyperplasia". Molecular Endocrinology 20, n.º 11 (1 de noviembre de 2006): 2946–64. http://dx.doi.org/10.1210/me.2006-0172.
Texto completoSantana, Margarida, Manuela M. Pereira, Nuno P. Elias, Cláudio M. Soares y Miguel Teixeira. "Gene Cluster of Rhodothermus marinusHigh-Potential Iron-Sulfur Protein:Oxygen Oxidoreductase, acaa3-Type Oxidase Belonging to the Superfamily of Heme-Copper Oxidases". Journal of Bacteriology 183, n.º 2 (15 de enero de 2001): 687–99. http://dx.doi.org/10.1128/jb.183.2.687-699.2001.
Texto completoScaffa, Alejandro, George A. Tollefson, Hongwei Yao, Salu Rizal, Joselynn Wallace, Nathalie Oulhen, Jennifer F. Carr, Katy Hegarty, Alper Uzun y Phyllis A. Dennery. "Identification of Heme Oxygenase-1 as a Putative DNA-Binding Protein". Antioxidants 11, n.º 11 (28 de octubre de 2022): 2135. http://dx.doi.org/10.3390/antiox11112135.
Texto completoTimmins, Amy y Sam P. de Visser. "A Comparative Review on the Catalytic Mechanism of Nonheme Iron Hydroxylases and Halogenases". Catalysts 8, n.º 8 (31 de julio de 2018): 314. http://dx.doi.org/10.3390/catal8080314.
Texto completoJortzik, Esther, Kathleen Zocher, Antje Isernhagen, Boniface M. Mailu, Stefan Rahlfs, Giampietro Viola, Sergio Wittlin, Nicholas H. Hunt, Heiko Ihmels y Katja Becker. "Benzo[b]quinolizinium Derivatives Have a Strong Antimalarial Activity and Inhibit Indoleamine Dioxygenase". Antimicrobial Agents and Chemotherapy 60, n.º 1 (12 de octubre de 2015): 115–25. http://dx.doi.org/10.1128/aac.01066-15.
Texto completoKrone, Nils, Yulia Grischuk, Marina Müller, Ruth Elisabeth Volk, Joachim Grötzinger, Paul-Martin Holterhus, Wolfgang G. Sippell y Felix G. Riepe. "Analyzing the Functional and Structural Consequences of Two Point Mutations (P94L and A368D) in the CYP11B1 Gene Causing Congenital Adrenal Hyperplasia Resulting from 11-Hydroxylase Deficiency". Journal of Clinical Endocrinology & Metabolism 91, n.º 7 (1 de julio de 2006): 2682–88. http://dx.doi.org/10.1210/jc.2006-0209.
Texto completoYadav, Rahul y Emily E. Scott. "Endogenous insertion of non-native metalloporphyrins into human membrane cytochrome P450 enzymes". Journal of Biological Chemistry 293, n.º 43 (14 de septiembre de 2018): 16623–34. http://dx.doi.org/10.1074/jbc.ra118.005417.
Texto completoAfonso, S. G., R. Enriquez de Salamanca y A. M. Del C. Batlle. "Porphyrin-induced protein structural alterations of heme enzymes". International Journal of Biochemistry & Cell Biology 29, n.º 8-9 (agosto de 1997): 1113–21. http://dx.doi.org/10.1016/s1357-2725(97)00045-9.
Texto completoShteinman, A. A. "Structural-functional modeling of non-heme oxygenases". Russian Chemical Bulletin 60, n.º 7 (julio de 2011): 1290–300. http://dx.doi.org/10.1007/s11172-011-0197-5.
Texto completoPiontek, K. "Structural biology of ligninolytic enzymes: laccases and heme peroxidases". Acta Crystallographica Section A Foundations of Crystallography 61, a1 (23 de agosto de 2005): c122. http://dx.doi.org/10.1107/s0108767305094857.
Texto completoZuccarello, Lidia, Catarina Barbosa, Smilja Todorovic y Célia M. Silveira. "Electrocatalysis by Heme Enzymes—Applications in Biosensing". Catalysts 11, n.º 2 (6 de febrero de 2021): 218. http://dx.doi.org/10.3390/catal11020218.
Texto completoNemukhin, A. V., B. L. Grigorenko, I. A. Topol y S. K. Burt. "Modeling dioxygen binding to the non-heme iron-containing enzymes". International Journal of Quantum Chemistry 106, n.º 10 (2006): 2184–90. http://dx.doi.org/10.1002/qua.20910.
Texto completoEmerson, Joseph P, Erik R Farquhar y Lawrence Que. "Structural “Snapshots” along Reaction Pathways of Non-Heme Iron Enzymes". Angewandte Chemie International Edition 46, n.º 45 (8 de octubre de 2007): 8553–56. http://dx.doi.org/10.1002/anie.200703057.
Texto completoMatsunaga, Isamu y Yoshitsugu Shiro. "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes". Current Opinion in Chemical Biology 8, n.º 2 (abril de 2004): 127–32. http://dx.doi.org/10.1016/j.cbpa.2004.01.001.
Texto completoPark, Hyunchang y Dongwhan Lee. "Ligand Taxonomy for Bioinorganic Modeling of Dioxygen‐Activating Non‐Heme Iron Enzymes". Chemistry – A European Journal 26, n.º 27 (17 de marzo de 2020): 5916–26. http://dx.doi.org/10.1002/chem.201904975.
Texto completoWu, Ruiying, Eric Patrick Skaar, Rongguang Zhang, Grazyna Joachimiak, Piotr Gornicki, Olaf Schneewind y Andrzej Joachimiak. "Staphylococcus aureusIsdG and IsdI, Heme-degrading Enzymes with Structural Similarity to Monooxygenases". Journal of Biological Chemistry 280, n.º 4 (31 de octubre de 2004): 2840–46. http://dx.doi.org/10.1074/jbc.m409526200.
Texto completoCarrasco, Maria C. y Shabnam Hematian. "(Hydr)oxo-bridged heme complexes: From structure to reactivity". Journal of Porphyrins and Phthalocyanines 23, n.º 11n12 (diciembre de 2019): 1286–307. http://dx.doi.org/10.1142/s1088424619300258.
Texto completoHa, Edward H., Raymond Y. N. Ho, James F. Kisiel y Joan Selverstone Valentine. "Modeling the Reactivity of .alpha.-Ketoglutarate-Dependent Non-Heme Iron(II)-Containing Enzymes". Inorganic Chemistry 34, n.º 9 (abril de 1995): 2265–66. http://dx.doi.org/10.1021/ic00113a002.
Texto completoZambrano, Gerardo, Emmanuel Ruggiero, Anna Malafronte, Marco Chino, Ornella Maglio, Vincenzo Pavone, Flavia Nastri y Angela Lombardi. "Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials". International Journal of Molecular Sciences 19, n.º 10 (24 de septiembre de 2018): 2896. http://dx.doi.org/10.3390/ijms19102896.
Texto completoValle-Altamirano, Rodolfo G., Maria Camilla Baratto, Isidro Badillo-Ramírez, Francisco Gasteazoro, Rebecca Pogni, José M. Saniger y Brenda Valderrama. "Identification of Fe(iii)–OH species as a catalytic intermediate in plant peroxidases at high H2O2 concentration". New Journal of Chemistry 46, n.º 10 (2022): 4579–86. http://dx.doi.org/10.1039/d1nj04837f.
Texto completoMukherjee, Jhumpa y Sriparna Ray. "Structurally Characterized Non-Heme Fe(IV)Oxo Complexes: A Brief Overview". Asian Journal of Chemistry 34, n.º 11 (2022): 2771–85. http://dx.doi.org/10.14233/ajchem.2022.23863.
Texto completoTodorovic, Smilja, Catarina Barbosa, Lidia Zuccarello y Celia M. Silveira. "Vibrational Spectro-Electrochemistry of Heme Proteins". ECS Meeting Abstracts MA2022-01, n.º 14 (7 de julio de 2022): 963. http://dx.doi.org/10.1149/ma2022-0114963mtgabs.
Texto completoSugimoto, Hiroshi, Youichi Naoe, Nozomi Nakamura, Akihiro Doi y Yoshitsugu Shiro. "Inward-facing conformation of the bacterial heme transporter". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C1500. http://dx.doi.org/10.1107/s205327331408499x.
Texto completoMirts, Evan N., Igor D. Petrik, Parisa Hosseinzadeh, Mark J. Nilges y Yi Lu. "A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme". Science 361, n.º 6407 (13 de septiembre de 2018): 1098–101. http://dx.doi.org/10.1126/science.aat8474.
Texto completoSiitonen, Vilja, Brinda Selvaraj, Laila Niiranen, Ylva Lindqvist, Gunter Schneider y Mikko Metsä-Ketelä. "Divergent non-heme iron enzymes in the nogalamycin biosynthetic pathway". Proceedings of the National Academy of Sciences 113, n.º 19 (25 de abril de 2016): 5251–56. http://dx.doi.org/10.1073/pnas.1525034113.
Texto completoLi, Huiying y Thomas L. Poulos. "Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures". Structure 2, n.º 6 (junio de 1994): 461–64. http://dx.doi.org/10.1016/s0969-2126(00)00046-0.
Texto completoGumiero, Andrea, Emma J. Murphy, Clive L. Metcalfe, Peter C. E. Moody y Emma Lloyd Raven. "An analysis of substrate binding interactions in the heme peroxidase enzymes: A structural perspective". Archives of Biochemistry and Biophysics 500, n.º 1 (agosto de 2010): 13–20. http://dx.doi.org/10.1016/j.abb.2010.02.015.
Texto completoCRISTINO, MARIA DA GLÓRIA G., CARLA CAROLINA F. DE MENESES, MALÚCIA MARQUES SOEIRO, JOÃO ELIAS V. FERREIRA, ANTONIO FLORÊNCIO DE FIGUEIREDO, JARDEL PINTO BARBOSA, RUTH C. O. DE ALMEIDA, JOSÉ C. PINHEIRO y ANDRÉIA DE LOURDES R. PINHEIRO. "COMPUTATIONAL MODELING OF ANTIMALARIAL 10-SUBSTITUTED DEOXOARTEMISININS". Journal of Theoretical and Computational Chemistry 11, n.º 02 (abril de 2012): 241–63. http://dx.doi.org/10.1142/s0219633612500162.
Texto completoLinde, Dolores, Elena Santillana, Elena Fernández-Fueyo, Alejandro González-Benjumea, Juan Carro, Ana Gutiérrez, Angel T. Martínez y Antonio Romero. "Structural Characterization of Two Short Unspecific Peroxygenases: Two Different Dimeric Arrangements". Antioxidants 11, n.º 5 (30 de abril de 2022): 891. http://dx.doi.org/10.3390/antiox11050891.
Texto completoRai, Amrita, Johann P. Klare, Patrick Y. A. Reinke, Felix Englmaier, Jörg Fohrer, Roman Fedorov, Manuel H. Taft et al. "Structural and Biochemical Characterization of a Dye-Decolorizing Peroxidase from Dictyostelium discoideum". International Journal of Molecular Sciences 22, n.º 12 (10 de junio de 2021): 6265. http://dx.doi.org/10.3390/ijms22126265.
Texto completoFix, Isabelle, Lorenz Heidinger, Thorsten Friedrich y Gunhild Layer. "The Radical SAM Heme Synthase AhbD from Methanosarcina barkeri Contains Two Auxiliary [4Fe-4S] Clusters". Biomolecules 13, n.º 8 (18 de agosto de 2023): 1268. http://dx.doi.org/10.3390/biom13081268.
Texto completoHagadorn, John R., Lawrence Que y William B. Tolman. "A Bulky Benzoate Ligand for Modeling the Carboxylate-Rich Active Sites of Non-Heme Diiron Enzymes". Journal of the American Chemical Society 120, n.º 51 (diciembre de 1998): 13531–32. http://dx.doi.org/10.1021/ja983333t.
Texto completoMahor, Durga, Julia Püschmann, Diederik R. Adema, Marc J. F. Strampraad y Peter-Leon Hagedoorn. "Unexpected photosensitivity of the well-characterized heme enzyme chlorite dismutase". JBIC Journal of Biological Inorganic Chemistry 25, n.º 8 (28 de octubre de 2020): 1129–38. http://dx.doi.org/10.1007/s00775-020-01826-8.
Texto completoSugishima, Masakazu, Kei Wada y Keiichi Fukuyama. "Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures". Current Medicinal Chemistry 27, n.º 21 (15 de junio de 2020): 3499–518. http://dx.doi.org/10.2174/0929867326666181217142715.
Texto completoSubedi, Pradeep, Hackwon Do, Jun Hyuck Lee y Tae-Jin Oh. "Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides". International Journal of Molecular Sciences 23, n.º 21 (1 de noviembre de 2022): 13317. http://dx.doi.org/10.3390/ijms232113317.
Texto completoGuleria, Praveen y Sudesh Kumar Yadav. "Insights into Steviol Glycoside Biosynthesis Pathway Enzymes Through Structural Homology Modeling". American Journal of Biochemistry and Molecular Biology 3, n.º 1 (15 de diciembre de 2012): 1–19. http://dx.doi.org/10.3923/ajbmb.2013.1.19.
Texto completoBabandi, Abba, Chioma A. Anosike, Lawrence U. S. Ezeanyika, Kemal Yelekçi y Abdullahi Ibrahim Uba. "Molecular modeling studies of some phytoligands from Ficus sycomorus fraction as potential inhibitors of cytochrome CYP6P3 enzyme of Anopheles coluzzii". Jordan Journal of Pharmaceutical Sciences 15, n.º 2 (1 de junio de 2022): 258–75. http://dx.doi.org/10.35516/jjps.v15i2.324.
Texto completoStiborová, Marie, Markéta Mikšanová, Václav Martínek y Eva Frei. "Heme Peroxidases: Structure, Function, Mechanism and Involvement in Activation of Carcinogens. A Review". Collection of Czechoslovak Chemical Communications 65, n.º 3 (2000): 297–325. http://dx.doi.org/10.1135/cccc20000297.
Texto completoHeider, Johann, Maciej Szaleniec, Katharina Sünwoldt y Matthias Boll. "Ethylbenzene Dehydrogenase and Related Molybdenum Enzymes Involved in Oxygen-Independent Alkyl Chain Hydroxylation". Journal of Molecular Microbiology and Biotechnology 26, n.º 1-3 (2016): 45–62. http://dx.doi.org/10.1159/000441357.
Texto completoOliveira, Ricardo N. S., Sara R. M. M. de Aguiar y Sofia R. Pauleta. "Coordination of the N-Terminal Heme in the Non-Classical Peroxidase from Escherichia coli". Molecules 28, n.º 12 (7 de junio de 2023): 4598. http://dx.doi.org/10.3390/molecules28124598.
Texto completoFranceschi, Lucia De, Mariarita Bertoldi, Maria Domenica Cappellini, Luigia De Falco, Sara Santos Franco, Luisa Ronzoni, Francesco Turrini, Alessandra Colancecco, Clara Camaschella y Achille Iolascon. "OXIDATIVE STRESS MODULATES HEME LEVELS and INDUCES PEROXIREDOXIN-2 IN β THALASSEMIC ERYTHROPOIESIS as NOVEL CYTOPROTECTIVE RESPONSE". Blood 116, n.º 21 (19 de noviembre de 2010): 4266. http://dx.doi.org/10.1182/blood.v116.21.4266.4266.
Texto completoChatfield, David C. y Alexander N. Morozov. "Influence of Conserved Structural Elements of the Proximal Pocket in HEME-Thiolate Enzymes on Oxygen Insertion Reactions". Biophysical Journal 114, n.º 3 (febrero de 2018): 585a. http://dx.doi.org/10.1016/j.bpj.2017.11.3202.
Texto completoAndersson, Laura A., Anna K. Johnson, Melissa D. Simms y Timothy R. Willingham. "Comparative analysis of catalases: spectral evidence against heme-bound water for the solution enzymes". FEBS Letters 370, n.º 1-2 (14 de agosto de 1995): 97–100. http://dx.doi.org/10.1016/0014-5793(95)00651-o.
Texto completoMajumdar, Amit y Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach". Coordination Chemistry Reviews 255, n.º 9-10 (mayo de 2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.
Texto completoZiemys, A. y J. Kulys. "Heme peroxidase clothing and inhibition with polyphenolic substances revealed by molecular modeling". Computational Biology and Chemistry 29, n.º 2 (abril de 2005): 83–90. http://dx.doi.org/10.1016/j.compbiolchem.2004.12.007.
Texto completoAbraham, Nader G., Jean-Michel Camadro, Sylvia T. Hoffstein y Richard D. Levere. "Effects of iron deficiency and chronic iron overloading on mitochondrial heme biosynthetic enzymes in rat liver". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 870, n.º 2 (marzo de 1986): 339–49. http://dx.doi.org/10.1016/0167-4838(86)90238-4.
Texto completoNóbrega, Cláudia S., Ana Luísa Carvalho, Maria João Romão y Sofia R. Pauleta. "Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase—Insights into the Catalytic Cycle of Bacterial Peroxidases". International Journal of Molecular Sciences 24, n.º 7 (26 de marzo de 2023): 6246. http://dx.doi.org/10.3390/ijms24076246.
Texto completoWan, Dun, Li Fu Liao y Ying Wu Lin. "Impacts of Uranyl Ion on the Structure and Function of Cytochrome b5 His39Ser Mutant". Advanced Materials Research 455-456 (enero de 2012): 1204–9. http://dx.doi.org/10.4028/www.scientific.net/amr.455-456.1204.
Texto completoHegg, Eric L. y Lawrence Que Jr. "The 2-His-1-Carboxylate Facial Triad - An Emerging Structural Motif in Mononuclear Non-Heme Iron(II) Enzymes". European Journal of Biochemistry 250, n.º 3 (diciembre de 1997): 625–29. http://dx.doi.org/10.1111/j.1432-1033.1997.t01-1-00625.x.
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