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Journal articles on the topic 'Cytochrome c Oxidase sunbunit I'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Sampson, Valerie, and Trevor Alleyne. "Cytochrome c /cytochrome c oxidase interaction." European Journal of Biochemistry 268, no. 24 (December 15, 2001): 6534–44. http://dx.doi.org/10.1046/j.0014-2956.2001.02608.x.

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2

Ostermeier, C. "Cytochrome c oxidase." Current Opinion in Structural Biology 6, no. 4 (August 1996): 460–66. http://dx.doi.org/10.1016/s0959-440x(96)80110-2.

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3

Shimokata, K., Y. Katayama, H. Shimada, and S. Yoshikawa. "hybrid cytochrome c oxidase." Seibutsu Butsuri 41, supplement (2001): S115. http://dx.doi.org/10.2142/biophys.41.s115_4.

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4

DiMAURO, SALVATORE, MASSIMO ZEVIANI, EDUARDO BONILLA, NEREO BRESOLIN, MASANORI NAKAGAWA, ARMAND F. MIRANDA, and MAURIZIO MOGGIO. "Cytochrome c oxidase deficiency." Biochemical Society Transactions 13, no. 4 (August 1, 1985): 651–53. http://dx.doi.org/10.1042/bst0130651.

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5

DiMauro, Salvatore, Anne Lombes, Hirofumi Nakase, Shuji Mita, Gian Maria Fabrizi, Eduardo Bonilla, Armand F. Miranda, Darryl C. DeVivo, and Eric A. Schon. "Cytochrome c Oxidase Deficiency." Pediatric Research 28, no. 5 (November 1990): 536–41. http://dx.doi.org/10.1203/00006450-199011000-00025.

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6

Shoubridge, Eric A. "Cytochrome c oxidase deficiency." American Journal of Medical Genetics 106, no. 1 (2001): 46–52. http://dx.doi.org/10.1002/ajmg.1378.

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7

Brischigliaro, Michele, and Massimo Zeviani. "Cytochrome c oxidase deficiency." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1862, no. 1 (January 2021): 148335. http://dx.doi.org/10.1016/j.bbabio.2020.148335.

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8

Antonini, G., M. Brunori, A. Colosimo, F. Malatesta, and P. Sarti. "Pulsed cytochrome c oxidase." Journal of Inorganic Biochemistry 23, no. 3-4 (March 1985): 289–93. http://dx.doi.org/10.1016/0162-0134(85)85037-6.

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9

Tsukihara, Tomitake. "Crystallographic studies of cytochrome c and cytochrome c oxidase." Journal of Biochemistry 171, no. 1 (October 26, 2021): 13–15. http://dx.doi.org/10.1093/jb/mvab118.

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10

Winterle, John S., and Ólöf Einarsdóttir. "Photoreactions of Cytochrome c Oxidase." Photochemistry and Photobiology 82, no. 3 (2006): 711. http://dx.doi.org/10.1562/2005-09-14-ra-684.

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11

SHINZAWA-ITOH, Kyoko. "Crystallization of Cytochrome c Oxidase." Nihon Kessho Gakkaishi 33, no. 5 (1991): 284–89. http://dx.doi.org/10.5940/jcrsj.33.284.

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12

BISSON, ROBERTO, and GIAMPIETRO SCHIAVO. "Slime Mold Cytochrome c Oxidase." Annals of the New York Academy of Sciences 550, no. 1 Cytochrome Ox (December 1988): 325–36. http://dx.doi.org/10.1111/j.1749-6632.1988.tb35347.x.

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13

Rak, Malgorzata, Paule Bénit, Dominique Chrétien, Juliette Bouchereau, Manuel Schiff, Riyad El-Khoury, Alexander Tzagoloff, and Pierre Rustin. "Mitochondrial cytochrome c oxidase deficiency." Clinical Science 130, no. 6 (February 4, 2016): 393–407. http://dx.doi.org/10.1042/cs20150707.

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Cytochrome oxidase defects are multiform diseases and despite major progress made in elucidating their molecular basis, we are still waiting for an efficient treatment. We discuss the cause of this discrepancy stressing the foremost questions that remain to be solved.

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14

Yoshikawa, Shinya. "Beef heart cytochrome c oxidase." Current Opinion in Structural Biology 7, no. 4 (August 1997): 574–79. http://dx.doi.org/10.1016/s0959-440x(97)80124-8.

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15

Khalimonchuk, Oleh, and Gerhard Rödel. "Biogenesis of cytochrome c oxidase." Mitochondrion 5, no. 6 (December 2005): 363–88. http://dx.doi.org/10.1016/j.mito.2005.08.002.

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16

Alleyne, Trevor, Damian Ashe, and Emmanuel Iwuoha. "Serum cytochrome c detection using a cytochrome c oxidase biosensor." Biotechnology and Applied Biochemistry 46, no. 4 (April 1, 2007): 185. http://dx.doi.org/10.1042/ba20060103.

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17

Pan, Lian Ping, James T. Hazzard, Jian Lin, Gordon Tollin, and Sunney I. Chan. "The electron input to cytochrome c oxidase from cytochrome c." Journal of the American Chemical Society 113, no. 15 (July 1991): 5908–10. http://dx.doi.org/10.1021/ja00015a081.

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18

Kornblatt, Jack A., Janice Theodorakis, Gaston Hui Bon Hoa, and Emmanuel Margoliash. "Cytochrome c and cytochrome c oxidase interactions: the effects of ionic strength and hydrostatic pressure studied with site-specific modifications of cytochrome c." Biochemistry and Cell Biology 70, no. 7 (July 1, 1992): 539–47. http://dx.doi.org/10.1139/o92-084.

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Seven cytochromes c, in which individual lysines have been modified to the propylthiobimane derivatives, have been prepared. These derivatives were also converted to the porphyrin cytochromes c by treatment with HF. The properties of both types of modified proteins were studied in their reactions with cytochrome c oxidase. The results show that lysines 25, 27, 60, 72, and 87 do not contribute a full charge to the binding interaction with the oxidase. These five residues, with the exception of the lysine-60 derivative, are on the front surface of the protein and contain the solvent-accessible edge of the heme prosthetic group. By contrast, lysines 8 and 13 at the top of the front surface do contribute a full charge to the binding interaction with the oxidase. The removal of the positive charge on any one lysine weakens the binding to cytochrome c oxidase by at least 1 kcal (1 cal = 4.1868 J). The presence of bimane at lysines 13 and 87 clearly forces the separation of the cytochrome c and oxidase, but this does not occur with the other complexes. The bimane-modified lysine-13 protein, and to a lesser extent that modified at lysine 8, show the interesting effect of enhanced complex formation with cytochrome c oxidase when subjected to pressure, possibly because of entrapment of water at the newly created interface of the complex. Our observations indicate that the two proteins of the cytochrome c – cytochrome oxidase complex have preferred, but not obligatory, spatial orientations and that interaction occurs without either protein losing significant portions of its hydration shell.Key words: cytochrome oxidase, cytochrome c, binding, hydrostatic pressure.

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19

Lynch, S. R., D. Sherman, and R. A. Copeland. "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase." Journal of Biological Chemistry 267, no. 1 (January 1992): 298–302. http://dx.doi.org/10.1016/s0021-9258(18)48493-1.

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20

KORNBLATT, Jack A., and Monique LABERGE. "Porphyrin cytochrome c. pH effects and interaction with cytochrome-c oxidase." European Journal of Biochemistry 175, no. 3 (August 1988): 475–79. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14219.x.

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21

Long, Russell C., Fred M. Hawkridge, and Charles R. Hartzell. "The indirect coulometric titration of cytochrome c oxidase with cytochrome c." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 198, no. 1 (January 1986): 89–98. http://dx.doi.org/10.1016/0022-0728(86)90028-8.

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22

Sharma, Vivek, and Mårten Wikström. "Oxidised states of cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863 (September 2022): 148671. http://dx.doi.org/10.1016/j.bbabio.2022.148671.

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23

Shimokata, K., Y. Katayama, H. Shimada, S. Nagano, Y. Ishimura, and S. Yoshikawa. "Reconstitution of bovine cytochrome c oxidase." Seibutsu Butsuri 39, supplement (1999): S121. http://dx.doi.org/10.2142/biophys.39.s121_2.

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24

Michel, Hartmut. "Proton pumping by cytochrome c oxidase." Nature 402, no. 6762 (December 1999): 602–3. http://dx.doi.org/10.1038/45133.

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25

ALLEYNE, TREVOR A., and MICHAEL T. WILSON. "Conformational changes in cytochrome c oxidase." Biochemical Society Transactions 15, no. 3 (June 1, 1987): 524–25. http://dx.doi.org/10.1042/bst0150524.

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26

Maurer, I., S. Zierz, H. J. Moller, and F. Jerusalem. "Cytochrome c oxidase in Alzheimer's disease." Neurology 45, no. 7 (July 1, 1995): 1423. http://dx.doi.org/10.1212/wnl.45.7.1423.

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27

Levy, Richard J., and Clifford S. Deutschman. "Cytochrome c oxidase dysfunction in sepsis." Critical Care Medicine 35, Suppl (September 2007): S468—S475. http://dx.doi.org/10.1097/01.ccm.0000278604.93569.27.

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28

DENIS, Michel, and Pierre RICHAUD. "Cytochrome c oxidase in plant mitochondria." European Journal of Biochemistry 147, no. 3 (June 28, 2008): 533–39. http://dx.doi.org/10.1111/j.0014-2956.1985.00533.x.

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29

Verkhovsky, Michael I., Audrius Jasaitis, Marina L. Verkhovskaya, Joel E. Morgan, and Mårten Wikström. "Proton translocation by cytochrome c oxidase." Nature 400, no. 6743 (July 1999): 480–83. http://dx.doi.org/10.1038/22813.

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30

Grossman, Lawrence I., and Margaret I. Lomax. "Nuclear genes for cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1352, no. 2 (May 1997): 174–92. http://dx.doi.org/10.1016/s0167-4781(97)00025-0.

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31

Lindsay, J. Gordon, Charles S. Owen, and David F. Wilson. "Azide binding to cytochrome c oxidase." Bioelectrochemistry and Bioenergetics 17, no. 3 (November 1987): 369–81. http://dx.doi.org/10.1016/0302-4598(87)80047-8.

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32

Wikström, Mårten, and Vivek Sharma. "Cytochrome c oxidase – a molecular machine." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (September 2018): e3. http://dx.doi.org/10.1016/j.bbabio.2018.09.007.

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33

Papa, Sergio, Nazzareno Capitanio, Giuseppe Capitanio, and Luigi L. Palese. "Protonmotive cooperativity in cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1658, no. 1-2 (July 2004): 95–105. http://dx.doi.org/10.1016/j.bbabio.2004.04.014.

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34

Yu, Michelle A., Tsuyoshi Egawa, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Syun-Ru Yeh, Denis L. Rousseau, and Gary J. Gerfen. "Radical formation in cytochrome c oxidase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1807, no. 10 (October 2011): 1295–304. http://dx.doi.org/10.1016/j.bbabio.2011.06.012.

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35

Yasunori, Shintani, Takaharu Hayashi, Yoshihiro Asano, and Seiji Takashima. "Higd1a Positively Regulates Cytochrome c oxidase." Journal of Cardiac Failure 21, no. 10 (October 2015): S174. http://dx.doi.org/10.1016/j.cardfail.2015.08.169.

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36

Rousseau, Denis L., Sanghwa Han, Sunho Song, and Yuan-Chin Ching. "Catalytic mechanism of cytochrome c oxidase." Journal of Raman Spectroscopy 23, no. 10 (October 1992): 551–56. http://dx.doi.org/10.1002/jrs.1250231007.

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37

Taanman, J. W., and S. L. Williams. "Assembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency?" Biochemical Society Transactions 29, no. 4 (August 1, 2001): 446–51. http://dx.doi.org/10.1042/bst0290446.

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Cytochrome c oxidase is an intricate metalloprotein that transfers electrons from cytochrome c to oxygen in the last step of the mitochondrial respiratory chain. It uses the free energy of this reaction to sustain a transmembrane electrochemical gradient of protons. Site-directed mutagenesis studies of bacterial terminal oxidases and the recent availability of refined crystal structures of the enzyme are rapidly expanding the understanding of the coupling mechanism between electron transfer and proton translocation. In contrast, relatively little is known about the assembly pathway of cytochrome c oxidase. Studies in yeast have indicated that assembly is dependent on numerous proteins in addition to the structural subunits and prosthetic groups. Human homologues of a number of these assembly factors have been identified and some are now known to be involved in disease. To dissect the assembly pathway of cytochrome c oxidase, we are characterizing tissues and cell cultures derived from patients with genetically defined cytochrome c oxidase deficiency, using biochemical, biophysical and immunological techniques. These studies have allowed us to identify some of the steps of the assembly process.

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38

Taanman, J. W., and S. L. Williams. "Assembly of cytochrome-c oxidase - What can we learn from patients with cytochrome-c oxidase deficiency?" Biochemical Society Transactions 29, no. 3 (June 1, 2001): A53. http://dx.doi.org/10.1042/bst029a053.

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39

Crum, John, Kenneth J. Gruys, and Terrence G. Frey. "Undecagold labeling of cytochrome c oxidase dimer crystals." Proceedings, annual meeting, Electron Microscopy Society of America 49 (August 1991): 278–79. http://dx.doi.org/10.1017/s0424820100085691.

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Cytochrome c oxidase (E.C. 1.9.3.1.) is an integral inner mitochondrial membrane protein, and is the terminal electron acceptor whereby cytochrome c (reduced by ubiquinol cytochrome c oxidoreductase) is oxidized and molecular oxygen is reduced producing water. When isolated mitochondria are treated with detergents, the other proteins and most of the lipids are extracted leaving membranous cytochrome c oxidase. Depending on the amounts and types of detergents used the cytochrome c oxidase molecules may form two-dimensional crystals composed of monomers or of dimers. These two-dimensional crystals are suitable for crystallographic image processing procedures. Recently the three-dimensional structure of cytochrome c oxidase in dimer crystals has been reported to a resolution of 20 Å. Though much work has been done, the location of the cytochrome c binding site on cytochrome c oxidase has not been determined.

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40

Kornblatt, Jack A., Mary Judith Kornblatt, Isabelle Rajotte, Gaston Hui Bon Hoa, and Peter C. Kahn. "Thermodynamic Volume Cycles for Electron Transfer in the Cytochrome c Oxidase and for the Binding of Cytochrome c to Cytochrome c Oxidase." Biophysical Journal 75, no. 1 (July 1998): 435–44. http://dx.doi.org/10.1016/s0006-3495(98)77531-9.

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41

Kossekova, G., B. Atanasov, R. Bolli, and A. Azzi. "Ionic-strength-dependence of the oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by cytochrome c oxidase." Biochemical Journal 262, no. 2 (September 1, 1989): 591–96. http://dx.doi.org/10.1042/bj2620591.

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The ionic-strength-dependences of the rate constants (log k plotted versus square root of 1) for oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by three different preparations of cytochrome c oxidase have complex non-linear character, which may be explained on the basis of present knowledge of the structure of the oxidase and the monomer-dimer equilibrium of the enzyme. The wave-type curve (with a minimum and a maximum) for oxidation of native cytochrome c by purified cytochrome c oxidase depleted of phospholipids may reflect consecutively inhibition of oxidase monomers (initial descending part), competition between this inhibition and dimer formation, resulting in increased activity (second part with positive slope), and finally inhibition of oxidase dimers (last descending part of the curve). The dependence of oxidation of native cytochrome c by cytochrome c oxidase reconstituted into phospholipid vesicles is a curve with a maximum, without the initial descending part described above. This may reflect the lack of pure monomers in the vesicles, where equilibrium is shifted to dimers even at low ionic strength. Subunit-III-depleted cytochrome c oxidase does not exhibit the maximum seen with the other two enzyme preparations. This may mean that removal of subunit III hinders dimer formation. The charge interactions of each of the cytochromes c (native or modified) with the three cytochrome c oxidase preparations are similar, as judged by the similar slopes of the linear dependences at I values above the optimal one. This shows that subunit III and the phospholipid membrane do not seem to be involved in the specific charge interaction of cytochrome c oxidase with cytochrome c.

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42

Hasinoff, B. B., and J. P. Davey. "The iron(III)-adriamycin complex inhibits cytochrome c oxidase before its inactivation." Biochemical Journal 250, no. 3 (March 15, 1988): 827–34. http://dx.doi.org/10.1042/bj2500827.

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Cytochrome c oxidase was found to be competitively inhibited by a complex formed between Fe3+ and the cardiotoxic antitumour drug adriamycin (doxorubicin) with an inhibition constant, Ki, of 12 microM. This competitive inhibition precedes the slower Fe3+-adriamycin induced inactivation of cytochrome c oxidase. In strong contrast with this result, free adriamycin was not observed to either inhibit or inactivate cytochrome c oxidase (Ki greater than 3 mM). Since, typically, polycations are known to inhibit cytochrome c oxidase, the competitive inhibition displayed by the Fe3+-adriamycin complex may also result from its polycationic character. Cytochrome c oxidase was also inhibited by pentan-1-ol (Ki 13 mM), and kinetic studies carried out in the presence of both inhibitors demonstrated that the Fe3+-adriamycin complex and pentan-1-ol are mutually exclusive inhibitors of cytochrome c oxidase. The inhibitor pentan-1-ol was also effective in preventing the slow inactivation of cytochrome c oxidase induced by Fe3+-adriamycin, presumably by blocking its binding to the enzyme. It is postulated that the slow inactivation of cytochrome c oxidase occurs when reactive radical species are produced while the Fe3+-adriamycin is complexed to cytochrome c oxidase in an enzyme-inhibitor complex. The Fe3+-adriamycin-induced inactivation of cytochrome c oxidase may be, in part, responsible for the cardiotoxicity of adriamycin.

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43

NICHOLLS, PETER, CHRISTIAN OBINGER, HELMUT NIEDERHAUSER, and GÜNTER A. PESCHEK. "Cytochrome c and c-554 oxidation by membranous Anacystis nidulans cytochrome oxidase." Biochemical Society Transactions 19, no. 3 (August 1, 1991): 252S. http://dx.doi.org/10.1042/bst019252s.

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44

Pan, Lian Ping, Sharon Hibdon, Rui Qin Liu, Bill Durham, and Francis Millett. "Intracomplex electron transfer between ruthenium-cytochrome c derivatives and cytochrome c oxidase." Biochemistry 32, no. 33 (August 24, 1993): 8492–98. http://dx.doi.org/10.1021/bi00084a014.

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45

Keenaway, Nancy G., Rooque D. Carrero-Valenzuela, Gary Ewart, Vijay K. Balan, Robert Lightowlers, Yu-Zhong Zhang, Berkley R. Powell, Roderick A. Capaldi, and Neil R. M. Buist. "Isoforms of Mammalian Cytochrome c Oxidase:Correlation with Human Cytochrome c Oxidase Deficiency." Pediatric Research 28, no. 5 (November 1990): 529–35. http://dx.doi.org/10.1203/00006450-199011000-00024.

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46

Young, L. J., and G. Palmer. "Redox-cycled oxidase. One of the reaction products of reduced cytochrome c, cytochrome c oxidase, and dioxygen." Journal of Biological Chemistry 261, no. 28 (October 1986): 13031–33. http://dx.doi.org/10.1016/s0021-9258(18)69266-x.

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47

Makino, Yoshio, Masayuki Ichimura, Yoshinori Kawagoe, and Seiichi Oshita. "Cytochrome c Oxidase as a Cause of Variation in Oxygen Uptake Rates Among Vegetables." Journal of the American Society for Horticultural Science 132, no. 2 (March 2007): 239–45. http://dx.doi.org/10.21273/jashs.132.2.239.

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The effect of cytochrome c oxidase, the terminal oxidase in the respiratory chain, on O2 uptake by vegetables was investigated. Broccoli florets (Brassica oleracea L. var. italica Plenck), spinach leaves (Spinacia oleracea L.), and onion bulbs (Allium cepa L.), which were expected to show rapid, moderate, and slow O2 uptake rates, respectively, were used in the current study. The order of O2 uptake rate measured by a closed method with a gas chromatograph was broccoli florets > spinach leaves > onion bulbs. Cytochrome c oxidase activity of mitochondrial preparations from onion bulbs was lower than that of the other vegetables, as was the O2 uptake rate. The higher O2 uptake rate of broccoli florets compared to spinach leaves was caused by higher cytochrome c oxidase activity of the floral buds. Grayscale luminance was used to determine the extent and distribution of staining in the tissues due to cytochrome c oxidase activity. Active O2 uptake by floral buds of broccoli florets was caused by the high concentration of cytochrome c oxidase in the pistil and petal. The absorbance of stems of broccoli florets at 823 nm, possibly derived from absorption by copper in cytochrome c oxidase, was higher than that of onion scale leaves, which agreed with the results of cytochrome c oxidase staining. We concluded that cytochrome c oxidase contributed to the O2 uptake rate by vegetables and that cytochrome c oxidase was one of the important causes for variation in O2 uptake rates among vegetables.

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48

Gnaiger, E., and A. V. Kuznetsov. "Mitochondrial respiration at low levels of oxygen and cytochrome c." Biochemical Society Transactions 30, no. 2 (April 1, 2002): 252–58. http://dx.doi.org/10.1042/bst0300252.

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In the intracellular microenvironment of active muscle tissue, high rates of respiration are maintained at near-limiting oxygen concentrations. The respiration of isolated heart mitochondria is a hyperbolic function of oxygen concentration and half-maximal rates were obtained at 0.4 and 0.7 μM O2 with substrates for the respiratory chain (succinate) and cytochrome c oxidase [N, N, N, N', N'-tetramethyl-p-phenylenediamine dihydrochloride (TMPD) + ascorbate] respectively at 30 °C and with maximum ADP stimulation (State 3). The respiratory response of cytochrome c-depleted mitoplasts to external cytochrome c was biphasic with TMPD, but showed a monophasic hyperbolic function with succinate. Half-maximal stimulation of respiration was obtained at 0.4 μM cytochrome c, which was nearly identical to the high-affinity K'm for cytochrome c of cytochrome c oxidase supplied with TMPD. The capacity of cytochrome c oxidase in the presence of TMPD was 2-fold higher than the capacity of the respiratory chain with succinate, measured at environmental normoxic levels. This apparent excess capacity, however, is significantly decreased under physiological intracellular oxygen conditions and declines steeply under hypoxic conditions. Similarly, the excess capacity of cytochrome c oxidase declines with progressive cytochrome c depletion. The flux control coefficient of cytochrome c oxidase, therefore, increases as a function of substrate limitation of oxygen and cytochrome c, which suggests a direct functional role for the apparent excess capacity of cytochrome c oxidase in hypoxia and under conditions of intracellular accumulation of cytochrome c after its release from mitochondria.

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49

Barrientos, Antoni, Danielle Pierre, Johnson Lee, and Alexander Tzagoloff. "Cytochrome oxidase assembly does not require catalytically active cytochrome c." Journal of Biological Chemistry 278, no. 43 (October 2003): 42728. http://dx.doi.org/10.1016/s0021-9258(20)82819-1.

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50

Cooper, Chris, Rebecca Holladay, Peter Nicholls, Dimitri Svistunenko, Maria Mason, Gary Silkstone, and Mike Wilson. "Nitric Oxide Interactions with Mitochondrial Cytochrome c and Cytochrome Oxidase." Free Radical Biology and Medicine 49 (January 2010): S10. http://dx.doi.org/10.1016/j.freeradbiomed.2010.10.682.

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