Mitochondrial dysfunction in patients with severe sepsis: An EPR interrogation of individual respiratory chain components

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 4, 2006, Pages 262-272

  Svistunenko, Dimitri A ^a   Davies, Nathan ^a   Brealey, David ^b   Singer, Mervyn ^b   Cooper, Chris E ^b  

^a UNIVERSITY OF ESSEX   (United Kingdom)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Complex I; EPR; Free radical; Iron sulfur; Mitochondria; Muscle; Sepsis

Indexed keywords

IRON SULFUR PROTEIN; RADICAL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SEMIQUINONE;

APACHE; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; CRITICAL ILLNESS; DISEASE SEVERITY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; HUMAN; HUMAN TISSUE; IN VIVO CULTURE; LOW TEMPERATURE; MUSCLE BIOPSY; OXIDATION REDUCTION REACTION; PATHOPHYSIOLOGY; PREDICTION; PRIORITY JOURNAL; RESPIRATORY CHAIN; SEPSIS; SEPTIC SHOCK; SPIN LABELING; TISSUE SECTION;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; HUMANS; MITOCHONDRIA; MUSCLES; SEPSIS;

EID: 33745212211     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.03.007     Document Type: Article

References (57)

1. Svistunenko D.A., Patel R.P., Voloshchenko S.V., and Wilson M.T. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 272 (1997) 7114-7121
2. Svistunenko D.A., Davies N.A., Wilson M.T., Stidwill R.P., Singer M., and Cooper C.E. Free radical in blood: a measure of haemoglobin autoxidation in vivo?. J. Chem. Soc., Perkin Trans. 2 (1997) 2539-2543
3. Svistunenko D.A., Dunne J., Fryer M., Nicholls P., Reeder B.J., Wilson M.T., Bigotti M.G., Cutruzzola F., and Cooper C.E. Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide. Biophys. J. 83 (2002) 2845-2855
4. Ohnishi T. Mitochondrial iron-sulfur flavodehydrogenases. Membrane Proteins in Energy Transduction (1979), Marcel Dekker, New York 1-87
5. Beinert H., and Albracht S.P. New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim. Biophys. Acta 683 (1982) 245-277
6. Commoner B., and Ternberg J.L. Free radicals in surviving tissues. Proc. Natl. Acad. Sci. U. S. A. 47 (1961) 1374-1384
7. Ruuge E.K., and Kornienko I.A. EPR spectra of frozen animal tissues [in Russ]. Biofizika 14 (1969) 752-754
8. Williams-Smith D.L., and Morrison P.J. Electron paramagnetic resonance spectra of catalase in mammalian tissues. Biochim. Biophys. Acta 405 (1975) 253-261
9. Burbaev D.S., Vanin A.F., Voevodskaia N.V., and Lebanidze A.V. EPR spectra of animal tissues in vitro [in Russ]. Biofizika 20 (1975) 1062-1067
10. Voevodskaia N.V., Burbaev D.S., Vanin A.F., and Blumenfeld L.A. EPR study of flavo- and ubisemiquinones in liver tissue [in Russ]. Mol. Biol. (Moskva) 15 (1981) 243-251
11. Pulatova M.K., Filatov D.E., Sharygin V.L., Gorbacheva L.B., Gudtsova K.V., Kuropteva Z.V., Zhumabaeva T.T., Shamaev V.I., and Korman D.B. The EPR spectra of the ribonucleotide reductase in the tumorous tissues and organs of tumor-bearing animals. Izv. Akad. Nauk SSSR, Biol. (1990) 737-748
12. Svistunenko D.A. Ascorbic acid radicals induced by the action of radiation in tissues from rat organs frozen at 77 K. Izv. Akad. Nauk SSSR, Biol. (1990) 827-834
13. Ruuge E.K., Ledenev A.N., Lakomkin V.L., Konstantinov A.A., and Ksenzenko M. Free radical metabolites in myocardium during ischemia and reperfusion. Am. J. Physiol. 261 (1991) 81-86
14. Premaratne S., Limm W., Mugiishi M.M., Piette L.H., and McNamara J.J. Quantitative assessment of free-radical generation during ischemia and reperfusion in the isolated rabbit heart. Coron. Artery Dis. 4 (1993) 1093-1096
15. Naughton D.P., and Symons M.C. When is a radical not a radical?. Free Radic. Res. 25 (1996) 1-3
16. Zecca L., and Swartz H.M. Total and paramagnetic metals in human substantia nigra and its neuromelanin. J. Neural Transm., Parkinson's Dis. Dement. Sect. 5 (1993) 203-3213
17. Swartz H.M., Liu K.J., Goda F., and Walczak T. India ink: a potential clinically applicable EPR oximetry probe. Magn. Reson. Med. 31 (1994) 229-232
18. Breen S.L., and Battista J.J. Radiation dosimetry in human bone using electron paramagnetic resonance. Phys. Med. Biol. 40 (1995) 2065-2077
19. Gorbunov N.V., Tyurina Y.Y., Salama G., Day B.W., Claycamp H.G., Argyros G., Elsayed N.M., and Kagan V.E. Nitric oxide protects cardiomyocytes against tert-butyl hydroperoxide-induced formation of alkoxyl and peroxyl radicals and peroxidation of phosphatidylserine. Biochem. Biophys. Res. Commun. 244 (1998) 647-651
20. Sok M., Sentjurc M., and Schara M. Membrane fluidity characteristics of human lung cancer. Cancer Lett. 139 (1999) 215-220
21. Svistunenko D.A., Sharpe M.A., Nicholls P., Wilson M.T., and Cooper C.E. A new method for quantitation of spin concentration by EPR spectroscopy: application to methemoglobin and metmyoglobin. J. Magn. Reson. 142 (2000) 266-275
22. Svistunenko D.A., Sharpe M.A., Nicholls P., Blenkinsop C., Davies N.A., Dunne J., Wilson M.T., and Cooper C.E. The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR study. Biochem. J. 351 (2000) 595-605
23. Svistunenko D.A. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins. Biochim. Biophys. Acta 1546 (2001) 365-378
24. McHugh J.P., Rodriguez-Quinones F., Abdul-Tehrani H., Svistunenko D.A., Poole R.K., Cooper C.E., and Andrews S.C. Global iron-dependent gene regulation in Escherichia coli. A new mechanism for iron homeostasis. J. Biol. Chem. 278 (2003) 29478-29486
25. Vanin A.F., Svistunenko D.A., Mikoyan V.D., Serezhenkov V.A., Fryer M.J., Baker N.R., and Cooper C.E. Endogenous superoxide production and the nitrite/nitrate ratio control the concentration of bioavailable free nitric oxide in leaves. J. Biol. Chem. 279 (2004) 24100-24107
26. Malone S.A., Lewin A., Kilic M.A., Svistunenko D.A., Cooper C.E., Wilson M.T., Le Brun N.E., Spiro S., and Moore G.R. Protein-template-driven formation of polynuclear iron species. J. Am. Chem. Soc. 126 (2004) 496-504
27. Brealey D., Brand M., Hargreaves I., Heales S., Land J., Smolenski R., Davies N.A., Cooper C.E., and Singer M. Association between mitochondrial dysfunction and severity and outcome of septic shock. Lancet 360 (2002) 219-223
28. Knaus W.A., Draper E.A., Wagner D.P., and Zimmerman J.E. APACHE II: a severity of disease classification system. Crit. Care Med. 13 (1985) 818-829
29. Peisach J., Blumberg W.E., Ogawa S., Rachmilewitz E.A., and Oltzik R. The effect of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance. J. Biol. Chem. 246 (1971) 3342-3355
30. Blumberg W.E., and Peisach J. A unified theory for low spin forms of all ferric heme proteins as studied by EPR. In: Chance B., Yonetani T., and Mildvan A.S. (Eds). Probes of structure and function of macromolecules and membranes (1971), Academic Press, New York 215-229
31. Peisach J., Blumberg W.E., Lode E.T., and Coon M.J. An analysis of the electron paramagnetic resonance spectrum of Pseudomonas oleovorans rubredoxin. A method for determination of the ligands of ferric iron in completely rhombic sites. J. Biol. Chem. 246 (1971) 5877-5881
32. Aisen P., Aasa R., Malmstrom B.G., and Vanngard T. Bicarbonate and the binding of iron to transferrin. J. Biol. Chem. 242 (1967) 2484-2490
33. Solomon E.I. Bioinorganic perspectives in copper coordination chemistry. In: Karlin K.D., and Zubieta J. (Eds). Copper coordination chemistry : biochemical and inorganic perspectives (1983), Adenine Press, Guilderland (NY) 1-22
34. Calabrese L., Carbonaro M., and Musci G. Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers. J. Biol. Chem. 263 (1988) 6480-6483
35. Cammack R., and Cooper C.E. Electron paramagnetic resonance spectroscopy of iron complexes and iron-containing proteins. Methods Enzymol. 227 (1993) 353-384
36. Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta 1364 (1998) 186-206
37. Berzofsky J.A., Peisach J., and Blumberg W.E. Sulfheme proteins: I. Optical and magnetic properties of sulfmyoglobin and its derivatives. J. Biol. Chem. 246 (1971) 3367-3377
38. Svistunenko D.A., Rob A., Ball A., Torres J., Symons M.C., Wilson M.T., and Cooper C.E. The electron paramagnetic resonance characterisation of a copper- containing extracellular peroxidase from Thermomonospora fusca BD25. Biochim. Biophys. Acta 1434 (1999) 74-85
39. Anemüller S., Hettmann T., Moll R., Teixeira M., and Schäfer G. EPR characterization of an archaeal succinate dehydrogenase in the membrane-bound state. Eur. J. Biochem. 232 (1995) 563-568
40. Schlenzka W., Shaw L., Kelm S., Schmidt C.L., Bill E., Trautwein A.X., Lottspeich F., and Schauer R. CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya. FEBS Lett. 385 (1996) 197-200
41. Ohnishi T., Sled V.D., Yano T., Yagi T., Burbaev D.S., and Vinogradov A.D. Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain. Biochim. Biophys. Acta 1365 (1998) 301-308
42. Ruzicka F.J., Beinert H., Schepler K.L., Dunham W.R., and Sands R.H. Interaction of ubisemiquinone with a paramagnetic component in heart tissue. Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2886-2890
43. Salerno J.C. Ohnishi, T. Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system. Biochem. J. 192 (1980) 769-781
44. Ingledew W.J., and Ohnishi T. Properties of the S-3 iron-sulphur centre of succinate dehydrogenase in the intact respiratory chain of beef heart mitochondria. FEBS Lett. 54 (1975) 167-171
45. Ingledew W.J., Salerno J.C., and Ohnishi T. Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier. Arch. Biochem. Biophys. 177 (1976) 176-184
46. Johnson M.K., Morningstar J.E., Bennett D.E., Ackrell B.A., and Kearney E.B. Magnetic circular dichroism studies of succinate dehydrogenase. Evidence for [2Fe-2S], [3Fe-xS], and [4Fe-4S] centers in reconstitutively active enzyme. J. Biol. Chem. 260 (1985) 7368-7378
47. Shergill J.K., Cammack R., Chen J.H., Fisher M.J., Madden S., and Rees H.H. EPR spectroscopic characterization of the iron-sulphur proteins and cytochrome P-450 in mitochondria from the insect Spodoptera littoralis (cotton leafworm). Biochem. J. 307 (1995) 719-728
48. Burbaev D.S., Vanin A.F., Sergeev A.I., Solojhenkin I.P., Volkova N.V., and Galperin E.I. The increase of oxidation level in the iron-sulphur proteins from the isolated tissues of mammals and patients under some pathologies. Stud. Biophys. 99 (1984) 143-150
49. Shergill J.K., Cammack R., Cooper C.E., Cooper J.M., Mann V.M., and Schapira A.H. Detection of nitrosyl complexes in human substantia nigra, in relation to Parkinson's disease. Biochem. Biophys. Res. Commun. 228 (1996) 298-305
50. Brealey D., Karyampudi S., Jacques T.S., Novelli M., Stidwill R., Taylor V., Smolenski R.T., and Singer M. Mitochondrial dysfunction in a long-term rodent model of sepsis and organ failure. Am. J. Physiol., Regul. Integr. Comp. Physiol. 286 (2004) R491-R497
51. Bolanos J.P., Almeida A., Stewart V., Peuchen S., Land J.M., Clark J.B., and Heales S.J. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J. Neurochem. 68 (1997) 2227-2240
52. Lambert A.J., and Brand M.D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279 (2004) 39414-39420
53. Beinert H., and Sands R.H. Biochem. Biophys. Res. Commun. 3 (1960) 41-45
54. Ohnishi T. Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart. Biochim. Biophys. Acta 387 (1975) 475-490
55. Albracht S.P., Dooijewaard G., Leeuwerik F.J., and Swol B.V. EPR signals of NADH: Q oxidoreductase. Shape and intensity. Biochim. Biophys. Acta 459 (1977) 300-317
56. Prince R.C., Lindsay J.G., and Dutton P.L. The Rieske iron-sulfur center in mitochondrial and photosynthetic systems: Em/pH relationships. FEBS Lett. 51 (1975) 108-111
57. Davidson E., Ohnishi T., Atta-Asafo-Adjei E., and Daldal F. Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of Rhodobacter capsulatus probed by site-directed mutagenesis. Biochemistry 31 (1992) 3342-3351