Relevant bibliographies by topics / Complexes of cytochrome c and cardiolipin

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Academic literature on the topic 'Complexes of cytochrome c and cardiolipin'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Complexes of cytochrome c and cardiolipin"

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Wang, Yujuan, and Junfeng Wang. "PB1F2 from Influenza A Virus Regulates the Interaction between Cytochrome C and Cardiolipin." Membranes 12, no. 8 (2022): 795. http://dx.doi.org/10.3390/membranes12080795.

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PB1F2 is a membrane associated protein encoded by the influenza virus gene in the host. Similar to endogenous pro-apoptotic proteins, it acts on the mitochondria of the host immune cells, inducing apoptosis of the cells. The PB1F2 protein has been demonstrated to facilitate the release of cytochrome c in addition to impairing the integrity of the inner mitochondrial membrane. This investigation focused on how the protein PB1F2 interacted with cardiolipin and cytochrome c. The regulation of PB1F2 on the binding of cytochrome c to cardiolipin in two kinds of in vitro membrane mimics was investig
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Reyna-Bolaños, Itzel, Elsa Paola Solís-García, Manuel Alejando Vargas-Vargas, et al. "Polydatin Prevents Electron Transport Chain Dysfunction and ROS Overproduction Paralleled by an Improvement in Lipid Peroxidation and Cardiolipin Levels in Iron-Overloaded Rat Liver Mitochondria." International Journal of Molecular Sciences 25, no. 20 (2024): 11104. http://dx.doi.org/10.3390/ijms252011104.

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Increased intramitochondrial free iron is a key feature of various liver diseases, leading to oxidative stress, mitochondrial dysfunction, and liver damage. Polydatin is a polyphenol with a hepatoprotective effect, which has been attributed to its ability to enhance mitochondrial oxidative metabolism and antioxidant defenses, thereby inhibiting reactive oxygen species (ROS) dependent cellular damage processes and liver diseases. However, it has not been explored whether polydatin is able to exert its effects by protecting the phospholipid cardiolipin against damage from excess iron. Cardiolipi
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Stepanov, G. O., G. K. Vladimirov, I. V. Kirilina, et al. "Stoichiometry of Formation of Physiologically Active Cytochrome C–Cardiolipin Complexes." Biophysics 70, no. 1 (2025): 63–68. https://doi.org/10.1134/s0006350925700083.

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Marchenkova, Margarita A., Yulia A. Dyakova, Elena Yu Tereschenko, Mikhail V. Kovalchuk, and Yury A. Vladimirov. "Cytochrome c Complexes with Cardiolipin Monolayer Formed under Different Surface Pressure." Langmuir 31, no. 45 (2015): 12426–36. http://dx.doi.org/10.1021/acs.langmuir.5b03155.

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Kapralov, Alexandr A., Naveena Yanamala, Yulia Y. Tyurina, et al. "Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c/cardiolipin peroxidase complexes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1808, no. 9 (2011): 2147–55. http://dx.doi.org/10.1016/j.bbamem.2011.04.009.

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Lopes, João, Dorinda Marques-da-Silva, Paula A. Videira, Alejandro K. Samhan-Arias, and Ricardo Lagoa. "Cardiolipin Membranes Promote Cytochrome c Transformation of Polycyclic Aromatic Hydrocarbons and Their In Vivo Metabolites." Molecules 29, no. 5 (2024): 1129. http://dx.doi.org/10.3390/molecules29051129.

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The catalytic properties of cytochrome c (Cc) have captured great interest in respect to mitochondrial physiology and apoptosis, and hold potential for novel enzymatic bioremediation systems. Nevertheless, its contribution to the metabolism of environmental toxicants remains unstudied. Human exposure to polycyclic aromatic hydrocarbons (PAHs) has been associated with impactful diseases, and animal models have unveiled concerning signs of PAHs’ toxicity to mitochondria. In this work, a series of eight PAHs with ionization potentials between 7.2 and 8.1 eV were used to challenge the catalytic ab
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Jiang, Jianfei, Ahmet Bakan, Alexandr A. Kapralov, et al. "Designing inhibitors of cytochrome c/cardiolipin peroxidase complexes: mitochondria-targeted imidazole-substituted fatty acids." Free Radical Biology and Medicine 71 (June 2014): 221–30. http://dx.doi.org/10.1016/j.freeradbiomed.2014.02.029.

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Канаровский, Е.Ю., О.В. Ялтыченко та Н.Н. Горинчой. "Кинетика антиоксидантной активности α-токоферола и некоторых его гомологов. Часть 1. Обзор проблемы. Теоретическая модель". Elektronnaya Obrabotka Materialov 53, № 5 (2017): 48–66. https://doi.org/10.5281/zenodo.1054137.

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It is presented the first part of the theoretical study devoted to the description of the kinetics and mechanism of the lipid peroxidation process involving the complexes of cytochrome <em>c</em> and cardiolipin, taking into account the effect of the antioxidant. The main components of the ROS (reactive oxygen species) and AOD (antioxidant defense) systems and their properties are considered. The key features of the functioning of these systems and various channels of the influence of their components on each other, both intra-systemic and inter-systemic, essential for the optimal interaction
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Capdevila, Daiana A., Santiago Oviedo Rouco, Florencia Tomasina, et al. "Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin." Biochemistry 54, no. 51 (2015): 7491–504. http://dx.doi.org/10.1021/acs.biochem.5b00922.

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ROUCOU, Xavier, Sylvie MONTESSUIT, Bruno ANTONSSON, and Jean-Claude MARTINOU. "Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein." Biochemical Journal 368, no. 3 (2002): 915–21. http://dx.doi.org/10.1042/bj20020972.

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In response to various apoptotic stimuli, Bax, a pro-apoptotic member of the Bcl-2 family, is oligomerized and permeabilizes the mitochondrial outer membrane to apoptogenic factors, including cytochrome c. Bax oligomerization can also be induced by incubating isolated mitochondria containing endogenous Bax with recombinant tBid (caspase-8-cleaved Bid) in vitro. The mechanism by which Bax oligomerizes under these conditions is still unknown. To address this question, recombinant human full-length Bax was purified as a monomeric protein. Bax failed to oligomerize spontaneously in isolated mitoch
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Dissertations / Theses on the topic "Complexes of cytochrome c and cardiolipin"

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Bataglioli, Daniela da Cunha. "Estudo da ligação do citocromo c a um modelo mimético de membrana mitocondrial contendo mono-hidroperóxido de cardiolipina." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-01102014-095441/.

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A interação do citocromo c com a cardiolipina ocorre por interações eletrostáticas e hidrofóbicas. A formação do complexo citocromo c/ cardiolipina promove uma pequena mudança estrutural na proteína, que proporciona atividade peroxidásica ao citocromo c e consequentemente capacidade de oxidar substratos orgânicos, incluindo a cardiolipina. A oxidação da cardiolipina acompanhada da inserção de um grupo peróxido vem sendo relacionada à perda da interação hidrofóbica entre o complexo citocromo c/cardiolipina, que resulta no desligamento do citocromo c da membrana e na sua saída do espaço intermem
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Saint-Georges, Chaumet Yann. "Contribution à l'étude de l'assemblage des complexes respiratoires chez Saccharomyces cerevisiae." Versailles-St Quentin en Yvelines, 2003. http://www.theses.fr/2003VERS0012.

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The biognesis of the respiratory complexes in mitochondria is an intricate process that need the Oxa1p function. In S. Cerevisiae, the introduction of residu baring a positive charge in the transmembrane domain of two subunits of complex III : cytochrome c1 and Qcr9p, is able to compensate for the complex IV misassembly, due to the absence of the protein Oxa1p. The study of the mechanism of suppression suggest interaction between these positive charges and negative ones localised in the transmembrane domain of subunit of complex IV, allowing their insertion in the membrane. Oxa1p could allow t
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Pathirathne, Thusitha. "Theoretical modeling of electron transfer rates between cytochrome c and small transition metal complexes a thesis presented to the faculty of the Graduate School, Tennessee Technological University /." Click to access online, 2009. http://proquest.umi.com/pqdweb?index=0&did=1760001881&SrchMode=1&sid=2&Fmt=6&VInst=PROD&VType=PQD&RQT=309&VName=PQD&TS=1268409541&clientId=28564.

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Alnajjar, Khadijeh Salim. "The Role of Subunit III in the Functional and Structural Regulation of Cytochrome c Oxidase in Rhodobacter spheroids." Wright State University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=wright1409219659.

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Pawlik, Grzegorz. "Assembly and maturation of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus." Thesis, Strasbourg, 2012. http://www.theses.fr/2012STRAF070.

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Dans cette thèse, le processus d'assemblage ainsi que la maturation du cytochrome c oxydase de type cbb3 (cbb3-Cox) ont été étudiés dans la proteobactérie phototrophique pourpe non soufrée Rhodobacter capsulatus. R. capsulatus contient une chaîne de transfert d'électrons très ramifiée et represente un modèle d’organisme très utilisé dans l'étude des processus respiratoires et photosynthétiques.Les cbb3-Coxs spécifiques des bactéries représentent la deuxième catégorie la plus abondante des cytochromes c oxydases après le type Cox-aa3, mais n'ont jusqu'à présent pas été étudiées en détail. Récem
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Hunt, Sheri A. "Deuterium NMR spectroscopy of solid state electronically labile complexes : mixed valence iron triangles, iron (II) spin crossover complexes and horse heart cytochrome c /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1997. http://wwwlib.umi.com/cr/ucsd/fullcit?p9804515.

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Perhirin, Antoine. "Interfaces électrochimiques appliquées à l'étude de composés d'intérêt biologique : application à l'étude de l'interaction entre cytochrome c et cardiolipide." Thesis, Brest, 2012. http://www.theses.fr/2012BRES0094/document.

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L’objectif de cette thèse était de mettre au point une interface électrochimique afin de caractériser les interactions entre le cytochrome c (cyt c), une protéine mitochondriale, et le cardiolipide (CL), un phospholipide présent dans les membranes des mitochondries. Le cyt c, dont la fonction est le transport d'électrons dans la chaîne respiratoire, est connu pour interagir avec le CL. Précédemment, un mécanisme d'accroche du cyt c sur une membrane contenant du CL a été mis en évidence par la théorie de l’« extented lipid anchorage ». Cette théorie prévoit, outre des interactions électrostatiq
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Jones, Torrie Turner. "Age-Related Deficits in Electron Transport Chain Complexes in Rat Neurons and 3xTg-AD Mouse Neurons." Available to subscribers only, 2009. http://proquest.umi.com/pqdweb?did=1797219571&sid=1&Fmt=2&clientId=1509&RQT=309&VName=PQD.

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Thesis (Ph. D.)--Southern Illinois University Carbondale, 2009.<br>"Department of Molecular Biology, Microbiology, and Biochemistry." Keywords: Aging, Cytochrome c oxidase, Electron transport chains, Estrogen, Mitochondria, Neurons. Includes bibliographical references (p. 102-137). Also available online.
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François-Moutal, Liberty. "Interactions protéines-membranes : conséquences sur l'état physique et l'organisation des lipides." Thesis, Lyon 1, 2013. http://www.theses.fr/2013LYO10062/document.

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Les isoenzymes de nucléoside diphosphate kinase (NDPK) sont connues depuis maintenant presque 60 ans et n'ont été considérées que pour leur activité catalytique de transfert de groupement phosphoryle. La découverte du gène nme, un gène antimétastatique codant une NDPK, a renouvelé l'intérêt scientifique pour cette famille d'enzymes. Il est désormais connu que la multiplication des gènes durant l'évolution a été accompagnée de diversifications structurales et fonctionnelles. J'ai étudié la fixation des NDPK-A, -B et –D (retrouvées associées aux membranes biologiques, bien que le rôle de cette a
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Sproch, Norman K. "Electrospray mass spectrometry : an investigation of non- covalent interactions of cytochrome c/crown ether complexes and applied methods of computational chemistry." Virtual Press, 1994. http://liblink.bsu.edu/uhtbin/catkey/917033.

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This research is directed at developing the interplay of experimental and computational methods in the area of biochemical mass spectrometry. The experimental method is that of electrospray ionization mass spectrometry (ESI-MS). The computational methods employed are those of semi-empirical quantum mechanics and molecular modeling.The use of Electrospray Mass Spectrometry was developed to investigate whole proteins and the non-covalent complexes that may be formed with small molecules. This method provides the soft ionization needed to accurately determine a noncovalently bound complex's mass
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Book chapters on the topic "Complexes of cytochrome c and cardiolipin"

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Kanarovskii, E. Yu, O. V. Yaltychenko, and N. N. Gorinchoy. "Theoretical Model of Lipid Peroxidation Kinetics for Complexes of Cytochrome c and Cardiolipin with Participation of Antioxidants." In IFMBE Proceedings. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-31866-6_100.

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Trivedi, A., A. V. Wearring, S. D. Kohlwein, F. Paltauf, and E. R. Tustanoff. "Functional Importance of Mitochondrial Cardiolipin in Yeast Cytochrome c Oxidase Activity." In Integration of Mitochondrial Function. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_9.

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Trivedi, A., M. Schwab, D. Fantin, and E. Reno Tustanoff. "Relationship of Cardiolipin to Cytochrome c Oxidase Kinetics as Probed by Adriamycin." In Membrane Receptors, Dynamics, and Energetics. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5335-5_27.

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Gorbenko, Galina P. "Fluorescence study of cytochrome C complexes with phospholipids." In Spectroscopy of Biological Molecules: New Directions. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4479-7_163.

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Sanders, Carsten, Serdar Turkarslan, Ozlem Onder, et al. "Biogenesis of c-type Cytochromes and Cytochrome Complexes." In The Purple Phototrophic Bacteria. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-1-4020-8815-5_21.

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Schmitt, Mark E., and Bernard L. Trumpower. "A Calmodulin-Like Protein in the Cytochrome bc1 Complex Required for Synthesis of both Cytochrome bc1 and Cytochrome c Oxidase Complexes in Yeast Mitochondria." In Cytochrome Systems. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_25.

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Matsuura, Katsumi, and Keizo Shimada. "Evolutionary Relationships between Reaction Center Complexes with and without Cytochrome c Subunits in Purple Bacteria." In Current Research in Photosynthesis. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_42.

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Khalfaoui-Hassani, Bahia, Andreia F. Verissimo, Namita P. Shroff, et al. "Biogenesis of Cytochrome c Complexes: From Insertion of Redox Cofactors to Assembly of Different Subunits." In Advances in Photosynthesis and Respiration. Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7481-9_27.

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Nanthakumar, Alaganandan, Stephen Fox, Sarwar M. Nasir, et al. "Dioxygen Reactivity Models for Cytochrome C Oxidase: Synthesis and Characterization of Oxo and Hydroxo-Bridged Porphyrin-Iron/Copper Dinuclear Complexes." In The Activation of Dioxygen and Homogeneous Catalytic Oxidation. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3000-8_27.

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Hough, Michael A., Gary Silkstone, J. A. R. Worrall, and Michael T. Wilson. "NO Binding to the Proapoptotic Cytochrome c–Cardiolipin Complex." In Vitamins & Hormones. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-800254-4.00008-8.

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Conference papers on the topic "Complexes of cytochrome c and cardiolipin"

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Levchenko, I. N., G. K. Vladimirov, and I. V. Volodyaev. "Study of the mechanism of reactions catalyzed by complexes of cytochrome C with cardiolipin." In Mathematical Biology and Bioinformatics. IMPB RAS - Branch of KIAM RAS, 2022. http://dx.doi.org/10.17537/icmbb22.19.

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Levchenko, I. N., G. K. Vladimirov, and I. V. Volodyaev. "STUDY OF THE MECHANISM OF PEROXIDASE ACTIVITY OF CYTOCHROME C IN COMPLEX WITH CARDIOLIPIN." In OpenBio-2023. ИПЦ НГУ, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-24.

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It is shown that: 1) the points of peroxidase activity and quantum yields are significantly higher in the presence of the natural dye coumarin C-334 than in the case of its own non-activated glow or in the case of the natural dye coumarin C-314; 2) peroxidase activity depends not only on the concentration of cytochrome C in the composition of the cytochrome C catalyst in combination with cardiolipin, but also on the relationship between the native form of cytochrome C and partially denatured.
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Levchenko, I. N., V. S. Pankratov, G. K. Vladimirov, A. A. Levchenko та I. V. Volodyaev. "STUDY OF THE STRUCTURE OF THE PORPHYRIN RING WITHIN THE CYTOCHROME С-CARDIOLIPIN-ACTIVATED COUMARIN С525 CHEMILUMINESCENCE UNDER THE ACTION OF THE COMPLEX". У XI МЕЖДУНАРОДНАЯ КОНФЕРЕНЦИЯ МОЛОДЫХ УЧЕНЫХ: БИОИНФОРМАТИКОВ, БИОТЕХНОЛОГОВ, БИОФИЗИКОВ, ВИРУСОЛОГОВ, МОЛЕКУЛЯРНЫХ БИОЛОГОВ И СПЕЦИАЛИСТОВ ФУНДАМЕНТАЛЬНОЙ МЕДИЦИНЫ. IPC NSU, 2024. https://doi.org/10.25205/978-5-4437-1691-6-28.

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Our results could become the basis for the creation of new drugs. Which are elements of the cell and have a therapeutic effect. Modulation and mathematical modeling of the porphyrin ring in as part of a heterogeneous catalyst of cytochrome C complex with cardiolipin, surrounded by a fluorescent probe of a physical activator of the natural dye coumarin С525 showed that the chemiluminescence of luminol is 3–4 orders of magnitude higher than that of the excited ketones, with cardiolipin itself being a “double” glycerophospholipid that is is considered a proton trap and has immune properties.
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Levchenko, I. N., I. V. Volodyaev, G. K. Vladimirov, and A. S. Boyarchenkov. "Mathematical modeling of quantum yields of chemiluminescence activated by coumarin C-525 under the action of a complex of cytochrome C with cardiolipin." In Mathematical Biology and Bioinformatics. IMPB RAS - Branch of KIAM RAS, 2022. http://dx.doi.org/10.17537/icmbb22.22.

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"Study of the mechanism of reactions catalyzed by complexes of cytochrome С with cardiolipin". У Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-123.

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