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

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Published: 3 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Kagan, V. E., Y. Y. Tyurina, H. Bayir, et al. "The “pro-apoptotic genies” get out of mitochondria: Oxidative lipidomics and redox activity of cytochrome c/cardiolipin complexes." Chemico-Biological Interactions 163, no. 1-2 (2006): 15–28. http://dx.doi.org/10.1016/j.cbi.2006.04.019.

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12

Sichevska, L. V., T. M. Ovsyannikova, A. O. Kovalenko, et al. "Influence of low-level laser radiation on the physico-chemical indicators of biomembranes." Biophysical Bulletin, no. 52 (December 25, 2024): 7–20. https://doi.org/10.26565/2075-3810-2024-52-01.

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Background: The study of physical and molecular mechanisms of the influence of low-level laser radiation (LLLR) of a wide frequency range on biological objects allows to clarify the problem of laser photomodulation at the level of natural biological membranes and their model analogues. Objectives: Identification of molecular and physical mechanisms of the influence of LLLR of a wide frequency range on biological objects of various levels of complexity. Materials and methods: Research objects: unicellular organisms S. cerevisiae, concentration of cells in the sample 18×106; model lipid membrane

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13

Vlasova, Irina. "Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control." Molecules 23, no. 10 (2018): 2561. http://dx.doi.org/10.3390/molecules23102561.

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The heme in the active center of peroxidases reacts with hydrogen peroxide to form highly reactive intermediates, which then oxidize simple substances called peroxidase substrates. Human peroxidases can be divided into two groups: (1) True peroxidases are enzymes whose main function is to generate free radicals in the peroxidase cycle and (pseudo)hypohalous acids in the halogenation cycle. The major true peroxidases are myeloperoxidase, eosinophil peroxidase and lactoperoxidase. (2) Pseudo-peroxidases perform various important functions in the body, but under the influence of external conditio

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14

Liu, Li, Lie Wu, Li Zeng, and Xiu-E. Jiang. "Label-free surface-enhanced infrared spectro-electro-chemical analysis of the Redox potential shift of cytochrome c complexed with a cardiolipin-containing lipid membrane of varied composition." Chinese Physics B 24, no. 12 (2015): 128201. http://dx.doi.org/10.1088/1674-1056/24/12/128201.

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15

Cardellach, F., T. F. Taraschi, J. S. Ellingson, C. D. Stubbs, E. Rubin, and J. B. Hoek. "Maintenance of structural and functional characteristics of skeletal-muscle mitochondria and sarcoplasmic-reticular membranes after chronic ethanol treatment." Biochemical Journal 274, no. 2 (1991): 565–73. http://dx.doi.org/10.1042/bj2740565.

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The effect of long-term ethanol intake on the structural and functional characteristics of rat skeletal-muscle mitochondria and sarcoplasmic reticulum was investigated. Functionally, skeletal-muscle mitochondria were characterized by a high respiratory control index and ADP/O ratio and a high State-3 respiration rate with different substrates. These parameters were not significantly different in preparations from control and ethanol-fed rats, except for a small increase in the rate of oxidation of alpha-oxoglutarate/malate in the latter. In submitochondrial particles from the two groups of ani

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16

Soussi, B., A. C. Bylund-Fellenius, T. Scherstén, and J. Ångström. "1H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals." Biochemical Journal 265, no. 1 (1990): 227–32. http://dx.doi.org/10.1042/bj2650227.

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The interaction between ferricytochrome c and cardiolipin was investigated by 1H n.m.r. at 270 MHz. From the phospholipid-induced changes of the protein spectral features it is concluded that the first 2 equivalents of cardiolipin cause a conformational change at the lower part of the solvent-exposed haem edge, involving a rearrangement of the hydrogen-bond interactions of propionate 6, thus partly accounting for the lowered redox potential of cytochrome c in the presence of cardiolipin. The increased value for the pK of the alkaline isomerization of ferricytochrome c shows that cardiolipin st

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17

Fiorucci, Laura, Fulvio Erba, Roberto Santucci, and Federica Sinibaldi. "Cytochrome c Interaction with Cardiolipin Plays a Key Role in Cell Apoptosis: Implications for Human Diseases." Symmetry 14, no. 4 (2022): 767. http://dx.doi.org/10.3390/sym14040767.

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In the cell cytochrome, c performs different functions depending on the environment in which it acts; therefore, it has been classified as a multifunction protein. When anchored to the outer side of the inner mitochondrial membrane, native cytochrome c acts as a Schweitzer-StennerSchweitzer-Stenner that transfers electrons from cytochrome c reductase to cytochrome c oxidase in the respiratory chain. On the other hand, to interact with cardiolipin (one of the phospholipids making up the mitochondrial membrane) and form the cytochrome c/cardiolipin complex in the apoptotic process, the protein r

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18

Lesnefsky, Edward J., Qun Chen, Thomas J. Slabe, et al. "Ischemia, rather than reperfusion, inhibits respiration through cytochrome oxidase in the isolated, perfused rabbit heart: role of cardiolipin." American Journal of Physiology-Heart and Circulatory Physiology 287, no. 1 (2004): H258—H267. http://dx.doi.org/10.1152/ajpheart.00348.2003.

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Ischemia and reperfusion result in mitochondrial dysfunction, with decreases in oxidative capacity, loss of cytochrome c, and generation of reactive oxygen species. During ischemia of the isolated perfused rabbit heart, subsarcolemmal mitochondria, located beneath the plasma membrane, sustain a loss of the phospholipid cardiolipin, with decreases in oxidative metabolism through cytochrome oxidase and the loss of cytochrome c. We asked whether additional injury to the distal electron chain involving cardiolipin with loss of cytochrome c and cytochrome oxidase occurs during reperfusion. Reperfus

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19

Ruiz-Ramírez, Angélica, Miguel-Angel Barrios-Maya, Ocarol López-Acosta, Dora Molina-Ortiz, and Mohammed El-Hafidi. "Cytochrome c release from rat liver mitochondria is compromised by increased saturated cardiolipin species induced by sucrose feeding." American Journal of Physiology-Endocrinology and Metabolism 309, no. 9 (2015): E777—E786. http://dx.doi.org/10.1152/ajpendo.00617.2014.

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Cytochrome c release from mitochondria has been described to be related to reactive oxygen species (ROS) generation. With ROS generation being increased in fatty liver from sucrose-fed (SF) rats, we hypothesized that cytochrome c release might be positively associated with H2O2 generation from SF mitochondria. Surprisingly, cytochrome c release from mitochondria of SF liver was found to be significantly lower compared with control (C) mitochondria oxidizing pyruvate/malate or succinate. Exposure of mitochondria to exogenous superoxide radical generated by the xanthine/xanthine oxidase system e

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20

Orrenius, Sten, and Boris Zhivotovsky. "Cardiolipin oxidation sets cytochrome c free." Nature Chemical Biology 1, no. 4 (2005): 188–89. http://dx.doi.org/10.1038/nchembio0905-188.

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21

Chertkova, Rita V., Alexander M. Firsov, Nadezda A. Brazhe та ін. "Multiple Mutations in the Non-Ordered Red Ω-Loop Enhance the Membrane-Permeabilizing and Peroxidase-like Activity of Cytochrome c". Biomolecules 12, № 5 (2022): 665. http://dx.doi.org/10.3390/biom12050665.

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A key event in the cytochrome c-dependent apoptotic pathway is the permeabilization of the outer mitochondrial membrane, resulting in the release of various apoptogenic factors, including cytochrome c, into the cytosol. It is believed that the permeabilization of the outer mitochondrial membrane can be induced by the peroxidase activity of cytochrome c in a complex with cardiolipin. Using a number of mutant variants of cytochrome c, we showed that both substitutions of Lys residues from the universal binding site for oppositely charged Glu residues and mutations leading to a decrease in the co

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22

Barayeu, Uladzimir, Mike Lange, Oleg Shadyro, Jürgen Arnhold, Jörg Flemmig, and Maria Fedorova. "Cytochrome c - cardiolipin interaction leads to the cytochrome c modification and degradation via formation of cardiolipin hydroperoxides." Free Radical Biology and Medicine 120 (May 2018): S76. http://dx.doi.org/10.1016/j.freeradbiomed.2018.04.251.

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23

Hanske, J., J. R. Toffey, A. M. Morenz, A. J. Bonilla, K. H. Schiavoni, and E. V. Pletneva. "Conformational properties of cardiolipin-bound cytochrome c." Proceedings of the National Academy of Sciences 109, no. 1 (2011): 125–30. http://dx.doi.org/10.1073/pnas.1112312108.

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24

Romodin, L. A. "On the use of cytochrome C as an anti-cancer agent." Veterinariya, Zootekhniya i Biotekhnologiya 1, no. 5 (2021): 6–13. http://dx.doi.org/10.36871/vet.zoo.bio.202105001.

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As means of cancer therapy, cytochrome C can be used, which can trigger a cascade of apoptotic reactions in the cytosol, as well as its complex with cardiolipin, which triggers lipid peroxidation, which can ultimately lead to cell death by the mechanism of apoptosis or ferroptosis. This article presents the possibility of using cytochrome C and its complex with phospholipids for the treatment of cancer, as well as the main problems associated with this. The main problem is the development of an effective means of delivering a cytotoxic agent to target cells in vivo. If all problems are solved,

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25

Gorbenko, Galyna P., Julian G. Molotkovsky, and Paavo K. J. Kinnunen. "Cytochrome c Interaction with Cardiolipin/Phosphatidylcholine Model Membranes: Effect of Cardiolipin Protonation." Biophysical Journal 90, no. 11 (2006): 4093–103. http://dx.doi.org/10.1529/biophysj.105.080150.

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26

Levchenko, I., G. Vladimirov, I. Volodyaev, and Yu Vladimirov. "FREE RADICALS. FEATURES OF CHEMILUMINESCENT ACTIVITY OF CYTOCHROME C CATALYST IN COMPLEX WITH CARDIOLIPIN." Russian Journal of Biological Physics and Chemisrty 8, no. 3 (2024): 277–81. http://dx.doi.org/10.29039/rusjbpc.2023.0621.

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Using the luminol chemiluminescence method for the lipid-membrane environment, which is condensed. Both lipid peroxidation processes, points of enzymatic activity, quantum yields, structure, and functions of the natural dye-activated fluorescent probe coumarin C-334 chemiluminescence under the action of a heterogeneous catalyst complex of cytochrome C with cardiolipin in aqueous medium and in a nonpolar environment were analyzed , and processes of lipid peroxidation, points of enzymatic activity, quantum yields, structure, functions of chemiluminescence activated by natural dye fluorescent pro

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27

Vladimirov, G. K., and I. V. Volodyaev. "STUDY THE ROLE OF CYTOCHROME C COMPLEX WITH CARDIOLIPIN IN THE CATALYSIS OF LIPID PEROXIDATION AND THE INITIATION OF APOPTOSIS: CALCULATION OF KINETIC CONSTANTS AND QUANTUM YIELDS BASED ON THE KINETICS OF ACTIVATED CHEMILUMINESCENCE." BIOTECHNOLOGY: STATE OF THE ART AND PERSPECTIVES 1, no. 2022-20 (2022): 55–58. http://dx.doi.org/10.37747/2312-640x-2022-20-55-58.

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Cytochrome c in a cell, in an aqueous medium or in a non-polar environment can be both in a free state and in complex with cardiolipin. In the latter case, it is partially denatured, characterized by a specific conformation, has peroxidase activity and is an important component of proapoptotic signaling pathways [1,2,9]. Differences between native cytochrome c and the cytochrome c—cardiolipin complex are recorded by the absorption and fluorescence spectra, as well as by the pronounced peroxidase activity of the latter and chemiluminescence accompanying the free radical processes it triggers. B

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28

Díaz-Quintana, Antonio, Gonzalo Pérez-Mejías, Alejandra Guerra-Castellano, Miguel A. De la Rosa, and Irene Díaz-Moreno. "Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin." Oxidative Medicine and Cellular Longevity 2020 (April 22, 2020): 1–20. http://dx.doi.org/10.1155/2020/6813405.

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Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor—cytochrome c—is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are inv

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29

Vikulina, A. S., A. V. Alekseev, E. V. Proskurnina, and Yu A. Vladimirov. "Cytochrome c–cardiolipin complex in a nonpolar environment." Biochemistry (Moscow) 80, no. 10 (2015): 1298–302. http://dx.doi.org/10.1134/s0006297915100107.

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30

Elmer-Dixon, Margaret M., Ziqing Xie, Jeremy B. Alverson, Nigel D. Priestley, and Bruce E. Bowler. "Curvature-Dependent Binding of Cytochrome c to Cardiolipin." Journal of the American Chemical Society 142, no. 46 (2020): 19532–39. http://dx.doi.org/10.1021/jacs.0c07301.

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31

Sinibaldi, Federica, Barry D. Howes, Enrica Droghetti, et al. "Role of Lysines in Cytochrome c–Cardiolipin Interaction." Biochemistry 52, no. 26 (2013): 4578–88. http://dx.doi.org/10.1021/bi400324c.

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32

Yurkova, Irina, Dominik Huster, and Juergen Arnhold. "Free radical fragmentation of cardiolipin by cytochrome c." Chemistry and Physics of Lipids 158, no. 1 (2009): 16–21. http://dx.doi.org/10.1016/j.chemphyslip.2008.09.005.

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33

Ascenzi, Paolo, Fabio Polticelli, Maria Marino, Roberto Santucci, and Massimo Coletta. "Cardiolipin drives cytochrome c proapoptotic and antiapoptotic actions." IUBMB Life 63, no. 3 (2011): 160–65. http://dx.doi.org/10.1002/iub.440.

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34

Levchenko, I. N., G. K. Vladimirov, I. V. Volodyaev, and Y. A. Vladimirov. "Peculiarities of Cytochrome c Enzymatic Activity with Cardiolipin." Moscow University Biological Sciences Bulletin 78, S1 (2023): S69—S71. http://dx.doi.org/10.3103/s0096392523700256.

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35

Butt, Julea N. "Explorations of time and electrochemical potential: opportunities for fresh perspectives on signalling proteins." Biochemical Society Transactions 42, no. 1 (2014): 47–51. http://dx.doi.org/10.1042/bst20130256.

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Apoptosis is triggered by an accumulation of ROS (reactive oxygen species) produced by proteins of the mitochondrial respiratory chain. The levels of ROS are controlled by the activities of mitochondrial redox proteins such as glutaredoxin 2 that help to modulate the susceptibility of a cell to apoptosis. However, once downstream events have resulted in the release of cytochrome c to the cytosol, it is widely considered that cell death is inevitable. Cytochrome c may promote its own release from mitochondria through interactions with the mitochondrial phospholipid cardiolipin (diphosphatidylgl

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36

Tang, Xiaofan, Lynda K. Harris, and Hui Lu. "Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1." International Journal of Molecular Sciences 21, no. 24 (2020): 9402. http://dx.doi.org/10.3390/ijms21249402.

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Erv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome c reductase activities. While both Erv1 and cytochrome c were reported to be membrane associated in mitochondria, it is unknown how the mitochondrial membrane environment may affect the function of Erv1. Here, in this study, we used liposomes to mimic the mitochondrial membrane and investigated the effect of liposomes and cardiolipin on the folding and function of yeast Erv1. Enzyme kinetics of both the oxid

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37

Abramovitch, Dorota A., Derek Marsh, and Gary L. Powell. "Activation of beef-heart cytochrome c oxidase by cardiolipin and analogues of cardiolipin." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1020, no. 1 (1990): 34–42. http://dx.doi.org/10.1016/0005-2728(90)90090-q.

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Josephs, Tracy M., Ian M. Morison, Catherine L. Day, Sigurd M. Wilbanks, and Elizabeth C. Ledgerwood. "Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: implications for the peroxidase mechanism and cytochrome c release." Biochemical Journal 458, no. 2 (2014): 259–65. http://dx.doi.org/10.1042/bj20131386.

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Enzymatic and mitochondrial release analyses of residue 41 variants of native and cardiolipin-bound mammalian cytochromes c implicate mobility of the 40–57 Ω loop in induction of peroxidase activity, but show that loss of axial Fe co-ordination is not essential.

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39

Rice, Malaysha, Bokey Wong, Mare Oja, et al. "A role of flavonoids in cytochrome c-cardiolipin interactions." Bioorganic & Medicinal Chemistry 33 (March 2021): 116043. http://dx.doi.org/10.1016/j.bmc.2021.116043.

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40

Bergstrom, C. L., P. A. Beales, Y. Lv, T. K. Vanderlick, and J. T. Groves. "Cytochrome c causes pore formation in cardiolipin-containing membranes." Proceedings of the National Academy of Sciences 110, no. 16 (2013): 6269–74. http://dx.doi.org/10.1073/pnas.1303819110.

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41

Ott, M., B. Zhivotovsky, and S. Orrenius. "Role of cardiolipin in cytochrome c release from mitochondria." Cell Death & Differentiation 14, no. 7 (2007): 1243–47. http://dx.doi.org/10.1038/sj.cdd.4402135.

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42

Miyamoto, Sayuri, Iseli L. Nantes, Priscila A. Faria, et al. "Cytochrome c-promoted cardiolipin oxidation generates singlet molecular oxygen." Photochemical & Photobiological Sciences 11, no. 10 (2012): 1536. http://dx.doi.org/10.1039/c2pp25119a.

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43

Muenzner, Julia, and Ekaterina V. Pletneva. "Structural transformations of cytochrome c upon interaction with cardiolipin." Chemistry and Physics of Lipids 179 (April 2014): 57–63. http://dx.doi.org/10.1016/j.chemphyslip.2013.11.002.

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Muenzner, Julia, Jason R. Toffey, Yuning Hong, and Ekaterina V. Pletneva. "Becoming a Peroxidase: Cardiolipin-Induced Unfolding of Cytochrome c." Journal of Physical Chemistry B 117, no. 42 (2013): 12878–86. http://dx.doi.org/10.1021/jp402104r.

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45

Yurchenko, A. A., P. D. Korotkova, V. I. Timofeev, A. B. Shumm, and Yu A. Vladimirov. "Modeling of the Interaction of Cytochrome c with Cardiolipin." Crystallography Reports 67, no. 6 (2022): 892–96. http://dx.doi.org/10.1134/s1063774522030257.

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46

Elmer-Dixon, Margaret M. "Elucidation of Electrostatic Determinants in Cytochrome C-Cardiolipin Binding." Biophysical Journal 110, no. 3 (2016): 421a—422a. http://dx.doi.org/10.1016/j.bpj.2015.11.2278.

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47

Barayeu, Uladzimir, Jörg Flemmig, Oleg Shadyro, and Jürgen Arnhold. "Cytochrome c- cardiolipin complex: from peroxidase to Fenton chemistry." Free Radical Biology and Medicine 108 (July 2017): S19. http://dx.doi.org/10.1016/j.freeradbiomed.2017.04.091.

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48

Robinson, Neal C., Jozef Zborowski, and Linda H. Talbert. "Cardiolipin-depleted bovine heart cytochrome c oxidase: binding stoichiometry and affinity for cardiolipin derivatives." Biochemistry 29, no. 38 (1990): 8962–69. http://dx.doi.org/10.1021/bi00490a012.

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Kim, Tae-Hyoung, Yongge Zhao, Wen-Xing Ding, et al. "Bid-Cardiolipin Interaction at Mitochondrial Contact Site Contributes to Mitochondrial Cristae Reorganization and Cytochrome c Release." Molecular Biology of the Cell 15, no. 7 (2004): 3061–72. http://dx.doi.org/10.1091/mbc.e03-12-0864.

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Abstract:

Release of cytochrome c from the mitochondrial intermembrane space is critical to apoptosis induced by a variety of death stimuli. Bid is a BH3-only prodeath Bcl-2 family protein that can potently activate this efflux. In the current study, we investigated the mitochondrial localization of Bid and its interactions with mitochondrial phospholipids, focusing on their relationships with Bid-induced cytochrome c release. We found that Bid binding to the mitochondria required only three of its eight helical structures (α4-α6), but not the BH3 domain, and the binding could not be inhibited by the an

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Schlame, Michael, Ivan Haller, Lisa Sammaritano, and Thomas Blanck. "Effect of Cardiolipin Oxidation on Solid-Phase Immunoassay for Antiphospholipid Antibodies." Thrombosis and Haemostasis 86, no. 12 (2001): 1475–82. http://dx.doi.org/10.1055/s-0037-1616751.

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Abstract:

SummaryDiagnostic assays for antiphospholipid antibodies are routinely performed on microtitre plates coated with cardiolipin. Here we show that contact between cardiolipin and NUNC-Immuno® plates leads to extensive oxidation, generating a series of peroxy-cardiolipins which were identified by electrospray ionization mass spectrometry. To investigate the impact of oxidation on the antibody assay, cardiolipin was resolved into 12 molecular species, including oxidized species and non-oxidized species with different degrees of unsaturation. All 12 species reacted under anaerobic conditions with s

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