메뉴 건너뛰기




Volumn 271, Issue 2 40-2, 1996, Pages

Reduction of cytochrome-c oxidase copper precedes failing cerebral O2 utilization in fluorocarbon-perfused cats

Author keywords

hypoxia; near infrared spectroscopy; perfluorocarbons; viscosity

Indexed keywords

ADENOSINE DIPHOSPHATE; COPPER; CYTOCHROME C OXIDASE; FLUOROCARBON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0029757473     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1996.271.2.h579     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0020479091 scopus 로고
    • Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c
    • Antalis, T. M., and G. Palmer. Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c. J. Biol. Chem. 257: 6194-6206, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6194-6206
    • Antalis, T.M.1    Palmer, G.2
  • 2
    • 0012422458 scopus 로고
    • Oxygen "pulsed" cytochrome c oxidase: Functional properties and catalytic relevance
    • Antonini, E., M. Brunori, A. Colosimo, C. Greenwood, and M. T. Wilson. Oxygen "pulsed" cytochrome c oxidase: functional properties and catalytic relevance. Proc. Natl. Acad. USA 74: 3128-3132, 1977.
    • (1977) Proc. Natl. Acad. USA , vol.74 , pp. 3128-3132
    • Antonini, E.1    Brunori, M.2    Colosimo, A.3    Greenwood, C.4    Wilson, M.T.5
  • 3
    • 0019319514 scopus 로고
    • Studies on the origin of the near-infrared (800-900 nm) absorption of cytochrome c oxidase
    • Beinert, H., R. W. Shaw, R. E. Hansen, and C. R. Hartzell. Studies on the origin of the near-infrared (800-900 nm) absorption of cytochrome c oxidase. Biochim. Biophys. Acta 591: 458-470, 1980.
    • (1980) Biochim. Biophys. Acta , vol.591 , pp. 458-470
    • Beinert, H.1    Shaw, R.W.2    Hansen, R.E.3    Hartzell, C.R.4
  • 4
    • 0017884616 scopus 로고
    • Functional studies on crosslinked bovine cytochrome c oxidase
    • Bonaventura, C., J. Bonaventura, M. Brunori, and M. Wilson. Functional studies on crosslinked bovine cytochrome c oxidase. FEBS Lett. 85: 30-34, 1978.
    • (1978) FEBS Lett. , vol.85 , pp. 30-34
    • Bonaventura, C.1    Bonaventura, J.2    Brunori, M.3    Wilson, M.4
  • 5
    • 0024406331 scopus 로고
    • Purification of cytochrome-c oxidase retaining its pulsed form
    • Brandt, U., H. Schagger, and G. von Jagow. Purification of cytochrome-c oxidase retaining its pulsed form. Eur. J. Biochem. 182: 705-711, 1989.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 705-711
    • Brandt, U.1    Schagger, H.2    Von Jagow, G.3
  • 6
    • 0018787610 scopus 로고
    • Functional intermediates of cytochrome oxidase Role of "pulsed" oxidase in the pre-steady state and steady state reactions of the beef enzyme
    • Brunori, M., A. Colosimo, G. Rainoni, M. T. Wilson, and E. Antonini. Functional intermediates of cytochrome oxidase Role of "pulsed" oxidase in the pre-steady state and steady state reactions of the beef enzyme. J. Biol. Chem. 254: 10769-10775. 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10769-10775
    • Brunori, M.1    Colosimo, A.2    Rainoni, G.3    Wilson, M.T.4    Antonini, E.5
  • 7
    • 0019885002 scopus 로고
    • "Pulsed" cytochrome oxidase may be produced without the advent of dioxygen
    • Brunori, M., A. Colosimo, P. Sarti, E. Antonini, and M. T. Wilson. "Pulsed" cytochrome oxidase may be produced without the advent of dioxygen. FEBS Lett. 126: 195-198, 1981.
    • (1981) FEBS Lett. , vol.126 , pp. 195-198
    • Brunori, M.1    Colosimo, A.2    Sarti, P.3    Antonini, E.4    Wilson, M.T.5
  • 8
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi, R. A. Structure and function of cytochrome c oxidase. Annu. Rev. Biochem. 59: 569-596, 1990.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 9
    • 0000862210 scopus 로고
    • Cellular oxygen requirements
    • Chance, B. Cellular oxygen requirements. Federation Proc. 16: 671-680, 1957.
    • (1957) Federation Proc. , vol.16 , pp. 671-680
    • Chance, B.1
  • 11
    • 0025634853 scopus 로고
    • Cerebral cytochrome-c oxidase copper band quantification in perfluorocarbon exchange transfused cats
    • Ferrari, M., D. F. Hanley, D. A. Wilson, and R. J. Traystman. Cerebral cytochrome-c oxidase copper band quantification in perfluorocarbon exchange transfused cats. Adv. Exp. Med. Biol. 277: 85-93, 1990.
    • (1990) Adv. Exp. Med. Biol. , vol.277 , pp. 85-93
    • Ferrari, M.1    Hanley, D.F.2    Wilson, D.A.3    Traystman, R.J.4
  • 12
    • 0025287119 scopus 로고
    • Redox changes in cat brain cytochrome-c oxidase after blood-fluorocarbon exchange
    • Heart Circ. Physiol. 27
    • Ferrari, M., D. F. Hanley, D. A. Wilson, and R. J. Traystman. Redox changes in cat brain cytochrome-c oxidase after blood-fluorocarbon exchange. Am. J. Physiol. 258 (Heart Circ. Physiol. 27): H1706-H1713, 1990.
    • (1990) Am. J. Physiol. , vol.258
    • Ferrari, M.1    Hanley, D.F.2    Wilson, D.A.3    Traystman, R.J.4
  • 13
    • 0028817444 scopus 로고
    • Redox changes in cat brain cytochrome-c oxidase after blood-fluorocarbon exchange during transient and graded hypoxia
    • Heart Circ. Physiol. 38
    • Ferrari, M., M. A. Williams, D. A. Wilson, N. V. Thakor, R. J. Traystman, and D. F. Hanley. Redox changes in cat brain cytochrome-c oxidase after blood-fluorocarbon exchange during transient and graded hypoxia. Am. J. Physiol. 269 (Heart Circ. Physiol. 38): H417-H424, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Ferrari, M.1    Williams, M.A.2    Wilson, D.A.3    Thakor, N.V.4    Traystman, R.J.5    Hanley, D.F.6
  • 14
    • 0022974929 scopus 로고
    • The proton-pumping site of cytochrome c oxidase: A model of its structure and mechanism
    • Gelles, J., D. F. Blair, and S. I. Chan. The proton-pumping site of cytochrome c oxidase: a model of its structure and mechanism Biochim. Biophys. Acta 853: 205-236, 1986.
    • (1986) Biochim. Biophys. Acta , vol.853 , pp. 205-236
    • Gelles, J.1    Blair, D.F.2    Chan, S.I.3
  • 15
    • 0022427471 scopus 로고
    • A center in cytochrome c oxidase by sodium p-(hydroxymercuri)benzoate
    • A center in cytochrome c oxidase by sodium p-(hydroxymercuri)benzoate. Biochemistry 24: 3963-3972, 1985.
    • (1985) Biochemistry , vol.24 , pp. 3963-3972
    • Gelles, J.1    Chan, S.I.2
  • 16
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • Groen, A. K., R. J. Wanders, H. V. Westerhoff, R. van der Meer, and J. M. Tager. Quantification of the contribution of various steps to the control of mitochondrial respiration. J. Biol. Chem. 257: 2754-2757, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.2    Westerhoff, H.V.3    Van Der Meer, R.4    Tager, J.M.5
  • 19
    • 0017571334 scopus 로고
    • Noninvasive, infrared monitoring of cerebral and myocardial oxygen sufficiency and circulatory parameters
    • Jöbsis, F. F. Noninvasive, infrared monitoring of cerebral and myocardial oxygen sufficiency and circulatory parameters. Science Wash. DC 198: 1264-1267, 1977.
    • (1977) Science Wash. DC , vol.198 , pp. 1264-1267
    • Jöbsis, F.F.1
  • 22
    • 0024284991 scopus 로고
    • Pressure-induced effects on cytochrome oxidase: The aerobic steady state
    • Kornblatt, J. A., G. Hui Bon Hoa, and K. Heremans. Pressure-induced effects on cytochrome oxidase: the aerobic steady state. Biochemistry 27: 5122-5128, 1988.
    • (1988) Biochemistry , vol.27 , pp. 5122-5128
    • Kornblatt, J.A.1    Hui Bon Hoa, G.2    Heremans, K.3
  • 24
    • 0023952584 scopus 로고
    • Effect of fluorocarbon-for-blood exchange on regional cerebral blood flow in rats
    • Heart Circ. Physiol. 23
    • Lee, P. A., A. L. Sylvia, and C. A. Piantadosi. Effect of fluorocarbon-for-blood exchange on regional cerebral blood flow in rats. Am. J. Physiol. 254 (Heart Circ. Physiol. 23): H719-H726, 1988.
    • (1988) Am. J. Physiol. , vol.254
    • Lee, P.A.1    Sylvia, A.L.2    Piantadosi, C.A.3
  • 25
    • 0026019550 scopus 로고
    • The detection of cytochrome oxidase heme iron and copper absorption in the blood-perfused and blood-free brain in normoxia and hypoxia
    • Miyake, H., S. Nioka, A. Zaman, D. S. Smith, and B. Chance. The detection of cytochrome oxidase heme iron and copper absorption in the blood-perfused and blood-free brain in normoxia and hypoxia. Anal. Biochem. 192: 149-155, 1991.
    • (1991) Anal. Biochem. , vol.192 , pp. 149-155
    • Miyake, H.1    Nioka, S.2    Zaman, A.3    Smith, D.S.4    Chance, B.5
  • 27
    • 0017615918 scopus 로고
    • EPR evidence for an active form of cytochrome c oxidase different from the resting enzyme
    • Rosen, S., R. Branden, T. Vanngard, and B, G. Malmstrom. EPR evidence for an active form of cytochrome c oxidase different from the resting enzyme. FEBS Lett. 74: 25-30, 1977.
    • (1977) FEBS Lett. , vol.74 , pp. 25-30
    • Rosen, S.1    Branden, R.2    Vanngard, T.3    Malmstrom, B.G.4
  • 28
    • 0023051673 scopus 로고
    • Two-electron reduction of cytochrome c oxidase triggers a conformational transition
    • Scholes, C. P., and B. G. Malmstrom. Two-electron reduction of cytochrome c oxidase triggers a conformational transition. FEBS Lett. 198: 125-129, 1986.
    • (1986) FEBS Lett. , vol.198 , pp. 125-129
    • Scholes, C.P.1    Malmstrom, B.G.2
  • 30
    • 0023818263 scopus 로고
    • 2 dependence of in vivo brain cytochrome redox responses and energy metabolism in bloodless rats
    • 2 dependence of in vivo brain cytochrome redox responses and energy metabolism in bloodless rats. J. Cereb. Blood Flow Metab. 8: 163-172, 1988.
    • (1988) J. Cereb. Blood Flow Metab. , vol.8 , pp. 163-172
    • Sylvia, A.L.1    Piantadosi, C.A.2
  • 31
    • 0010981084 scopus 로고
    • Studies on the electron transfer system. LVII. The near-infrared absorption band of cytochrome oxidase
    • Wharton, D. C., and A. Tzagoloff. Studies on the electron transfer system. LVII. The near-infrared absorption band of cytochrome oxidase. J. Biol. Chem. 239: 2036-2040, 1964.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2036-2040
    • Wharton, D.C.1    Tzagoloff, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.