دورية أكاديمية

Effect of the mitochondrial membrane potential on the absorbance of the reduced form of cytochrome c oxidase.

التفاصيل البيبلوغرافية
العنوان: Effect of the mitochondrial membrane potential on the absorbance of the reduced form of cytochrome c oxidase.
المؤلفون: Covian R; Laboratory of Cardiac Energetics and Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, United States of America., Edwards LO; Laboratory of Cardiac Energetics and Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, United States of America., Balaban RS; Laboratory of Cardiac Energetics and Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, United States of America.
المصدر: Biochimica et biophysica acta. Bioenergetics [Biochim Biophys Acta Bioenerg] 2024 Aug 01; Vol. 1865 (3), pp. 149048. Date of Electronic Publication: 2024 May 07.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731706 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-2650 (Electronic) Linking ISSN: 00052728 NLM ISO Abbreviation: Biochim Biophys Acta Bioenerg Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam : Elsevier
مواضيع طبية MeSH: Electron Transport Complex IV*/metabolism , Membrane Potential, Mitochondrial*/drug effects , Mitochondria, Heart*/enzymology , Mitochondria, Heart*/metabolism, Animals ; Rabbits ; Oxidation-Reduction ; Cyanides/pharmacology ; Cyanides/metabolism
مستخلص: The effect of mitochondrial membrane potential (ΔΨ m ) on the absorbance of the reduced cytochrome c oxidase (COX) was evaluated in isolated rabbit heart mitochondria using integrating sphere optical spectroscopy. Maximal reduction of the mitochondrial cytochromes was achieved by either blowing nitrogen to remove oxygen, or by adding cyanide. Gradual depolarization of ΔΨ m by adding increasing concentrations of uncoupler resulted in an increase of up to 50 % in the absorbance of cytochrome aa 3 under nitrogen saturation, and of 25 % with cyanide. Cytochrome aa 3 absorbance increases were also observed in the presence of cyanide with apyrase (20 %) or oligomycin (12 %). The b L heme absorbance also decreased as expected from ΔΨ m depolarization. A ~ 1 nm red shift in the peak wavelength of cytochrome aa 3 was observed under anoxic conditions as ΔΨ m was depolarized. Importantly, cytochrome c and c 1 absorbances remained constant at levels corresponding to full reduction under all experimental manipulations of ΔΨ m , especially with cyanide. These data suggest that ΔΨ m -dependent changes in the absorbance of reduced COX were due to a variable extinction coefficient of heme a and/or a 3 as a function of ΔΨ m . A similar increase in the reduced cytochrome aa 3 absorbance without changes in cytochrome c and c 1 was observed in the perfused rabbit heart when decreasing ΔΨ m with uncoupler. Our results imply that COX absorbance in its fully reduced state does not simply reflect the oxygen tension but also the ΔΨ m . This may prove useful in monitoring ΔΨ m under anoxic or ischemic conditions in intact tissue.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Published by Elsevier B.V.)
References: Circ Res. 2021 May 14;128(10):1487-1513. (PMID: 33983836)
Am J Physiol Heart Circ Physiol. 2017 Dec 1;313(6):H1199-H1208. (PMID: 28939647)
J Biol Chem. 1983 Dec 25;258(24):14908-13. (PMID: 6317678)
Biochem Soc Trans. 2017 Jun 15;45(3):813-829. (PMID: 28620043)
Am J Physiol. 1997 Feb;272(2 Pt 2):H769-75. (PMID: 9124437)
Biochemistry. 1970 Dec 22;9(26):5077-82. (PMID: 4320585)
Am J Physiol Cell Physiol. 2000 Feb;278(2):C423-35. (PMID: 10666039)
Biochim Biophys Acta Bioenerg. 2023 Apr 1;1864(2):148934. (PMID: 36379270)
Am J Physiol Cell Physiol. 2011 Jun;300(6):C1280-90. (PMID: 21289287)
Anal Biochem. 2013 Aug 15;439(2):161-72. (PMID: 23665273)
Anal Biochem. 2019 Dec 1;586:113443. (PMID: 31539522)
Am J Physiol Heart Circ Physiol. 2018 Apr 1;314(4):H704-H715. (PMID: 29127235)
Biochim Biophys Acta Bioenerg. 2018 Aug;1859(8):555-566. (PMID: 29704499)
Biochim Biophys Acta. 2011 Jul;1807(7):779-87. (PMID: 21420929)
Biochim Biophys Acta. 1996 Jun 13;1274(3):109-11. (PMID: 8664303)
Anal Biochem. 1996 Jun 1;237(2):274-8. (PMID: 8660576)
Chem Rev. 2018 Mar 14;118(5):2469-2490. (PMID: 29350917)
J Clin Invest. 2022 May 16;132(10):. (PMID: 35575090)
Biophys J. 2012 Mar 7;102(5):1194-203. (PMID: 22404942)
معلومات مُعتمدة: Z01 HL004601 United States ImNIH Intramural NIH HHS; Z99 HL999999 United States ImNIH Intramural NIH HHS
فهرسة مساهمة: Keywords: Cytochrome c oxidase; Heart; Membrane potential; Mitochondria; Respiration; Spectroscopy; electron transfer
المشرفين على المادة: EC 1.9.3.1 (Electron Transport Complex IV)
0 (Cyanides)
تواريخ الأحداث: Date Created: 20240509 Date Completed: 20240609 Latest Revision: 20240620
رمز التحديث: 20240620
مُعرف محوري في PubMed: PMC11181927
DOI: 10.1016/j.bbabio.2024.149048
PMID: 38723704
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-2650
DOI:10.1016/j.bbabio.2024.149048