Specificity of lipids and coenzyme Q in mitochondrial NADH and succin-oxidase of beef heart and S. cerevisiae |
| |
| Authors: | G Lenaz A Castelli G P Littarru E Bertoli |
| |
| Affiliation: | 1. Graduate School of International Agricultural Technology, Seoul National University, Pyeongchang 25354, Republic of Korea;2. Institutes of Green Bio Science and Technology, Seoul National University, Pyeongchang 25354, Republic of Korea;3. Department of Animal Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea;1. Animal Science Research Institute of Iran (ASRI), Agricultural Research Education and Extension Organization (AREEO), Tehran, Iran;2. Department of Poultry Science, Faculty of Agriculture, Tarbiat Modares University, Tehran, Iran;3. Department of Animal Science, University College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran;1. Wellcome Trust Centre for Mitochondrial Research, Institute of Neuroscience, Newcastle University, Newcastle upon Tyne NE2 4HH, UK;2. The Medical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK;3. Department of Life Sciences, University of Parma, Parco Area delle Scienze 11A, Parma 43124, Italy;4. Department of Pediatrics, Institute of Clinical Medicine, University of Tartu, 51014 Tartu, Estonia;5. Department of Genetics, United Laboratories, Tartu University Hospital, 51014 Tartu, Estonia;6. Manchester Centre for Genomic Medicine, Central Manchester University Hospitals NHS Foundation Trust, St Marys Hospital, Oxford Road, Manchester M13 9WL, UK;7. Paediatric Neurology Unit, “Dana” Children Hospital, Tel Aviv Sourasky Medical Centre, Sackler Faculty of Medicine, Tel Aviv University, 64239 Tel Aviv, Israel;8. Department of Respiratory Rehabilitation, Alyn Hospital, Jerusalem 91090, Israel;9. Metabolic Laboratory Department of Genetics and Metabolic Diseases, Hadassah-Hebrew University Medical Center, Jerusalem 91120, Israel;10. Neonatal Intensive Care Unit, “Lis” Maternity Hospital, Tel Aviv Sourasky Medical Centre, 64239 Tel Aviv, Israel;11. Research Programs Unit, Molecular Neurology, Biomedicum-Helsinki, University of Helsinki, 00290 Helsinki, Finland;12. Department of Pediatric Neurology, Children’s Hospital, Helsinki University Hospital and University of Helsinki, 00290 Helsinki, Finland;13. Department of Paediatric Inherited Metabolic Diseases, Evelina Children’s Hospital, London SE1 7EH, UK;14. Division of Genetics and Molecular Medicine, King’s College London School of Medicine, London SE1 9RY, UK;15. Clinical Genetics Unit, Guys and St Thomas’ NHS Foundation Trust, London SE1 9RT, UK;16. Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA;17. Radboud Center for Mitochondrial Medicine, Department of Paediatrics, Translational Metabolic Laboratory, Radboud University Medical Centre, 6525 GA Nijmegen, the Netherlands;18. Department of Neurosciences, Helsinki University Hospital and University of Helsinki, 00290 Helsinki, Finland;19. The Monique and Jacques Roboh Department of Genetic Research, Hadassah-Hebrew University Medical Center, Jerusalem 91120, Israel |
| |
| Abstract: | The organic structural specificity of coenzyme Q in NADH- and succin-oxidase has been studied with mitochondria from the yeast, S. cerevisiae, and compared with the specificity for mitochondrial enzyme systems from beef heart. The specificity of lipids in CoQ-enzyme systems has also been studied. The origin and concentration of micellar phospholipids used as carriers for the CoQ homologs profoundly affects the restoration of NADH-oxidase in pentane-extracted mitochondria both from yeast and beef heart. High concentrations of phospholipids induce a decrease of the NADH-oxidase activity which had been restored by the lower homologs of CoQ. The activity with CoQ1-CoQ4 was higher than that with the natural CoQ6 in yeast mitochondria, and was lower than that with the natural CoQ10 in beef heart mitochondria, irrespective of the concentration of phospholipids. Mitochondrial phospholipids of yeast were more effective than soybean phospholipids in supporting restoration of NADH-oxidase by the higher homologs in pentane-extracted mitochondria of yeast. This difference was not evident for succin-oxidase from yeast and beef heart. Succin-oxidase from both sources was similarly restored by the homologs CoQ2-Q10 independently of the phospholipid concentration.According to these data, there are two sites for CoQ6 in yeast mitochondria as there are two sites for CoQ10 in beef heart mitochondria. The nature of the site in NADH-oxidase of yeast and of beef heart is different. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
