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Volumn 1817, Issue 4, 2012, Pages 672-679

Kinetic studies of the reactions of O 2 and NO with reduced Thermus thermophilus ba 3 and bovine aa 3 using photolabile carriers

Author keywords

CO photodissociation; Double laser transient absorption spectroscopy; O 2 and NO photolabile carriers; Thermus thermophilus ba 3

Indexed keywords

AA3 OXIDASE; BA3 OXIDASE; CARBON MONOXIDE; COPPER ION; HEME A3; HEME DERIVATIVE; NITRIC OXIDE; OXIDOREDUCTASE; OXYGEN; UNCLASSIFIED DRUG;

EID: 84857913919     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.12.005     Document Type: Review
Times cited : (23)

References (57)
  • 1
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • P. Brzezinski, and G. Larsson Redox-driven proton pumping by heme-copper oxidases Biochim. Biophys. Acta 1605 2003 1 13
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 2
  • 3
    • 78650545848 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in cytochrome oxidase
    • V.R. Kaila, M.I. Verkhovsky, and M. Wikström Proton-coupled electron transfer in cytochrome oxidase Chem. Rev. 110 2010 7062 7081
    • (2010) Chem. Rev. , vol.110 , pp. 7062-7081
    • Kaila, V.R.1    Verkhovsky, M.I.2    Wikström, M.3
  • 4
    • 0028955899 scopus 로고
    • Fast reactions of cytochrome oxidase
    • Ó. Einarsdóttir Fast reactions of cytochrome oxidase Biochim. Biophys. Acta 1229 1995 129 147
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 129-147
    • Einarsdóttir, Ó.1
  • 5
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M.K.F. Wikström Proton pump coupled to cytochrome c oxidase in mitochondria Nature 266 1977 271 273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.F.1
  • 6
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance
    • C.E. Cooper, and G.C. Brown The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance J. Bioenerg. Biomembr. 40 2008 533 539
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 7
    • 31444433077 scopus 로고    scopus 로고
    • Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase
    • M.G. Mason, P. Nicholls, M.T. Wilson, and C.E. Cooper Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 103 2006 708 713
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 708-713
    • Mason, M.G.1    Nicholls, P.2    Wilson, M.T.3    Cooper, C.E.4
  • 9
  • 12
  • 16
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 18
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Törnroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 20
    • 2042528736 scopus 로고
    • Spectroscopy, dynamics, and function of cytochrome oxidase
    • R.J.H. Clark, R.E. Hester, John Wiley and Sons Ltd Chichester, England
    • W.H. Woodruff, R.B. Dyer, and Ó. Einarsdóttir Spectroscopy, dynamics, and function of cytochrome oxidase R.J.H. Clark, R.E. Hester, Biological Spectroscopy, Part B 1993 John Wiley and Sons Ltd Chichester, England 189 233
    • (1993) Biological Spectroscopy, Part B , pp. 189-233
    • Woodruff, W.H.1    Dyer, R.B.2    Einarsdóttir, Ó.3
  • 21
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Q.H. Gibson, and C. Greenwood Reactions of cytochrome oxidase with oxygen and carbon monoxide Biochem. J. 86 1963 541 554
    • (1963) Biochem. J. , vol.86 , pp. 541-554
    • Gibson, Q.H.1    Greenwood, C.2
  • 27
    • 0026038522 scopus 로고
    • Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase
    • R.S. Blackmore, C. Greenwood, and Q.H. Gibson Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase J. Biol. Chem. 266 1991 19245 19249
    • (1991) J. Biol. Chem. , vol.266 , pp. 19245-19249
    • Blackmore, R.S.1    Greenwood, C.2    Gibson, Q.H.3
  • 33
    • 0028021633 scopus 로고
    • Time-resolved optical absorption studies of intramolecular electron transfer in cytochrome c oxidase
    • K.E. Georgiadis, N.-I. Jhon, and Ó. Einarsdóttir Time-resolved optical absorption studies of intramolecular electron transfer in cytochrome c oxidase Biochemistry 33 1994 9245 9256
    • (1994) Biochemistry , vol.33 , pp. 9245-9256
    • Georgiadis, K.E.1    Jhon, N.-I.2    Einarsdóttir, Ó.3
  • 34
    • 0025105229 scopus 로고
    • Nanosecond photolysis of rhodopsin: Evidence for a new, blue-shifted intermediate
    • S.J. Hug, J.W. Lewis, C.M. Einterz, T.E. Thorgeirsson, and D.S. Kliger Nanosecond photolysis of rhodopsin: evidence for a new, blue-shifted intermediate Biochemistry 29 1990 1475 1485
    • (1990) Biochemistry , vol.29 , pp. 1475-1485
    • Hug, S.J.1    Lewis, J.W.2    Einterz, C.M.3    Thorgeirsson, T.E.4    Kliger, D.S.5
  • 35
    • 0030749599 scopus 로고    scopus 로고
    • Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates
    • I. Szundi, J.W. Lewis, and D.S. Kliger Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates Biophys. J. 73 1997 688 702
    • (1997) Biophys. J. , vol.73 , pp. 688-702
    • Szundi, I.1    Lewis, J.W.2    Kliger, D.S.3
  • 36
    • 0037657608 scopus 로고    scopus 로고
    • PH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 2. Branched electron transfer pathways linked by proton transfer
    • I. Szundi, N. Van Eps, and Ó. Einarsdóttir pH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 2. Branched electron transfer pathways linked by proton transfer Biochemistry 42 2003 5074 5090
    • (2003) Biochemistry , vol.42 , pp. 5074-5090
    • Szundi, I.1    Van Eps, N.2    Einarsdóttir, Ó.3
  • 37
    • 0028013676 scopus 로고
    • Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase
    • R.B. Dyer, K.A. Peterson, P.O. Stoutland, and W.H. Woodruff Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase Biochemistry 33 1994 500 507
    • (1994) Biochemistry , vol.33 , pp. 500-507
    • Dyer, R.B.1    Peterson, K.A.2    Stoutland, P.O.3    Woodruff, W.H.4
  • 38
    • 61449231809 scopus 로고    scopus 로고
    • Accommodation of two diatomic molecules in cytochrome bo: Insights into NO reductase activity in terminal oxidases
    • T. Hayashi, M.T. Lin, K. Ganesan, Y. Chen, J.A. Fee, R.B. Gennis, and P. Moenne-Loccoz Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases Biochemistry 48 2009 883 890
    • (2009) Biochemistry , vol.48 , pp. 883-890
    • Hayashi, T.1    Lin, M.T.2    Ganesan, K.3    Chen, Y.4    Fee, J.A.5    Gennis, R.B.6    Moenne-Loccoz, P.7
  • 42
    • 0344961407 scopus 로고    scopus 로고
    • Ligand binding in a docking site of cytochrome c oxidase: A time-resolved step-scan Fourier transform infrared study
    • C. Koutsoupakis, T. Soulimane, and C. Varotsis Ligand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan Fourier transform infrared study J. Am. Chem. Soc. 125 2003 14728 14732
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14728-14732
    • Koutsoupakis, C.1    Soulimane, T.2    Varotsis, C.3
  • 46
    • 0011539080 scopus 로고
    • The orientation of CO in carbonmonoxy cytochrome oxidase and its transient photoproducts. Direct evidence from time-resolved infrared linear dichroism
    • R.B. Dyer, J.J. López-Garriga, Ó. Einarsdóttir, and W.H. Woodruff The orientation of CO in carbonmonoxy cytochrome oxidase and its transient photoproducts. Direct evidence from time-resolved infrared linear dichroism J. Am. Chem. Soc. 111 1989 8962 8963
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8962-8963
    • Dyer, R.B.1    López-Garriga, J.J.2    Einarsdóttir, Ó.3    Woodruff, W.H.4
  • 49
    • 42349083650 scopus 로고    scopus 로고
    • 3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • 3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases Biochemistry 47 2008 4657 4665
    • (2008) Biochemistry , vol.47 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2    Fee, J.A.3    Stout, C.D.4
  • 50
    • 4143060405 scopus 로고    scopus 로고
    • A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter
    • L. Salomonsson, A. Lee, R.B. Gennis, and P. Brzezinski A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter Proc. Natl. Acad. Sci. U. S. A. 101 2004 11617 11621
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11617-11621
    • Salomonsson, L.1    Lee, A.2    Gennis, R.B.3    Brzezinski, P.4
  • 53
    • 1942472472 scopus 로고    scopus 로고
    • Time-resolved optical absorption studies of cytochrome oxidase dynamics
    • Ó. Einarsdóttir, and I. Szundi Time-resolved optical absorption studies of cytochrome oxidase dynamics Biochim. Biophys. Acta 1655 2004 263 273
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 263-273
    • Einarsdóttir, Ó.1    Szundi, I.2
  • 54
    • 0037799915 scopus 로고    scopus 로고
    • R state is a pH-dependent mixture of three intermediates, A, P, and F
    • R state is a pH-dependent mixture of three intermediates, A, P, and F Biochemistry 42 2003 5065 5073
    • (2003) Biochemistry , vol.42 , pp. 5065-5073
    • Van Eps, N.1    Szundi, I.2    Einarsdóttir, Ó.3
  • 56
    • 0032558999 scopus 로고    scopus 로고
    • Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen
    • A. Sucheta, I. Szundi, and Ó. Einarsdóttir Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen Biochemistry 37 1998 17905 17914
    • (1998) Biochemistry , vol.37 , pp. 17905-17914
    • Sucheta, A.1    Szundi, I.2    Einarsdóttir, Ó.3
  • 57
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • M.I. Verkhovsky, J.E. Morgan, and M. Wikström Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase Biochemistry 33 1994 3079 3086
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3


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