메뉴 건너뛰기




Volumn 1706, Issue 1-2, 2005, Pages 126-133

Characterization of steady-state activities of cytochrome c oxidase at alkaline pH: Mimicking the effect of K-channel mutations in the bovine enzyme

Author keywords

Alkaline pH value; Circular dichroism; Cytochrome c; Cytochrome c oxidase; Peroxidase; Steady state kinetics

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C OXIDASE; HEART ENZYME; HEME; HYDROGEN PEROXIDE; POTASSIUM CHANNEL;

EID: 11144249354     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.10.002     Document Type: Article
Times cited : (9)

References (48)
  • 1
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • S. Ferguson-Miller, and G. Babcock Heme/copper terminal oxidases Chem. Rev. 96 1996 2889 2907
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.2
  • 2
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • M. Saraste Structural features of cytochrome oxidase Q. Rev. Biophys. 23 1990 331 366
    • (1990) Q. Rev. Biophys. , vol.23 , pp. 331-366
    • Saraste, M.1
  • 3
    • 0018185852 scopus 로고
    • Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles
    • K. Krab, and M. Wikström Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles Biochim. Biophys. Acta 504 1978 200 214
    • (1978) Biochim. Biophys. Acta , vol.504 , pp. 200-214
    • Krab, K.1    Wikström, M.2
  • 4
    • 0020724790 scopus 로고
    • Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoresis procedure
    • B. Kadenbach, J. Jarausch, R. Hartmann, and P. Merle Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoresis procedure Anal. Biochem. 129 1983 517 521
    • (1983) Anal. Biochem. , vol.129 , pp. 517-521
    • Kadenbach, B.1    Jarausch, J.2    Hartmann, R.3    Merle, P.4
  • 6
    • 0020491044 scopus 로고
    • The cytochrome c peroxidase activity of cytochrome oxidase
    • Y. Orii The cytochrome c peroxidase activity of cytochrome oxidase J. Biol. Chem. 257 1982 9246 9248
    • (1982) J. Biol. Chem. , vol.257 , pp. 9246-9248
    • Orii, Y.1
  • 7
    • 0035859920 scopus 로고    scopus 로고
    • Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide
    • C. Pecoraro, R.B. Gennis, T.V. Vygodina, and A.A. Konstantinov Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide Biochemistry 40 2001 9695 9708
    • (2001) Biochemistry , vol.40 , pp. 9695-9708
    • Pecoraro, C.1    Gennis, R.B.2    Vygodina, T.V.3    Konstantinov, A.A.4
  • 8
    • 0020709955 scopus 로고
    • Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c
    • F. Millett, C. de Jong, L. Paulsen, and R. Capaldi Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c Biochemistry 22 1983 546 552
    • (1983) Biochemistry , vol.22 , pp. 546-552
    • Millett, F.1    De Jong, C.2    Paulsen, L.3    Capaldi, R.4
  • 9
    • 0017253440 scopus 로고
    • Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase
    • S. Ferguson-Miller, D.L. Brautigan, and E. Margoliash Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase J. Biol. Chem. 251 1976 1104 1115
    • (1976) J. Biol. Chem. , vol.251 , pp. 1104-1115
    • Ferguson-Miller, S.1    Brautigan, D.L.2    Margoliash, E.3
  • 12
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • A.A. Konstantinov, S. Siletsky, D. Mitchell, A. Kaulen, and R.B. Gennis The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer Proc. Natl. Acad. Sci. U. S. A. 94 1997 9085 9090
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 13
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully reduced enzyme with dioxygen
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully reduced enzyme with dioxygen Biochemistry 36 1997 13824 13829
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ådelroth, P.1    Svensson-Ek, M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 14
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems, and postulates
    • D. Zaslavsky, and R.B. Gennis Proton pumping by cytochrome oxidase: progress, problems, and postulates Biochim. Biophys. Acta 1458 2000 164 179
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 16
    • 0032478132 scopus 로고    scopus 로고
    • Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochrome c oxidase
    • T.V. Vygodina, C. Pecoraro, D. Mitchell, R. Gennis, and A.A. Konstantinov Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochrome c oxidase Biochemistry 37 1998 3053 3061
    • (1998) Biochemistry , vol.37 , pp. 3053-3061
    • Vygodina, T.V.1    Pecoraro, C.2    Mitchell, D.3    Gennis, R.4    Konstantinov, A.A.5
  • 17
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K (I-362) in proton transfer in cytochrome c oxidase from Rhodobacter sphaeroides
    • P. Ådelroth, R.B. Gennis, and P. Brzezinski Role of the pathway through K (I-362) in proton transfer in cytochrome c oxidase from Rhodobacter sphaeroides Biochemistry 37 1998 2470 2476
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ådelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 18
    • 0039840998 scopus 로고    scopus 로고
    • Effects of the mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • S. Jünemann, B. Meunier, R.B. Gennis, and P.R. Rich Effects of the mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides Biochemistry 36 1997 14456 14464
    • (1997) Biochemistry , vol.36 , pp. 14456-14464
    • Jünemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 19
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determined the transition rates between oxygen intermediates in cytochrome c oxidase
    • P. Ådelroth, M. Karpefors, G. Gilderson, F.L. Tomson, R.B. Gennis, and P. Brzezinski Proton transfer from glutamate 286 determined the transition rates between oxygen intermediates in cytochrome c oxidase Biochim. Biophys. Acta 1459 2000 533 539
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 533-539
    • Ådelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 20
    • 0019317708 scopus 로고
    • The effect of pH and ionic strength on the steady-state activity of isolated cytochrome c oxidase
    • J. Wilms, J.L.M.L. Van Rijn, and B.F. Van Gelder The effect of pH and ionic strength on the steady-state activity of isolated cytochrome c oxidase Biochim. Biophys. Acta 593 1980 17 23
    • (1980) Biochim. Biophys. Acta , vol.593 , pp. 17-23
    • Wilms, J.1    Van Rijn, J.L.M.L.2    Van Gelder, B.F.3
  • 21
    • 0023046076 scopus 로고
    • The effects of pH and ionic strength on cytochrome c oxidase steady-state kinetics reveal a catalytic and a non-catalytic interaction domain for cytochrome c
    • K.M.C. Sinjorgo, O.M. Steinbach, H.L. Dekker, and A.O. Muijsers The effects of pH and ionic strength on cytochrome c oxidase steady-state kinetics reveal a catalytic and a non-catalytic interaction domain for cytochrome c Biochim. Biopys. Acta 850 1986 108 115
    • (1986) Biochim. Biopys. Acta , vol.850 , pp. 108-115
    • Sinjorgo, K.M.C.1    Steinbach, O.M.2    Dekker, H.L.3    Muijsers, A.O.4
  • 22
    • 0018338653 scopus 로고
    • Preparation of bovine heart mitochondria in high yield
    • G.F. Azzone, R. Colanna, and B. Ziche Preparation of bovine heart mitochondria in high yield Methods Enzymol. 55 1971 46 50
    • (1971) Methods Enzymol. , vol.55 , pp. 46-50
    • Azzone, G.F.1    Colanna, R.2    Ziche, B.3
  • 23
    • 77957006730 scopus 로고
    • Cytochrome oxidase: Beef heart
    • T. Yonetani Cytochrome oxidase: beef heart Methods Enzymol. 10 1967 332 335
    • (1967) Methods Enzymol. , vol.10 , pp. 332-335
    • Yonetani, T.1
  • 24
    • 0027731932 scopus 로고
    • Detection of bovine heart mitochondrial cytochrome c oxidase dimers in triton X-100 and phospholipid vesicles by chemical cross-linking
    • L. Estey, and L.J. Prochaska Detection of bovine heart mitochondrial cytochrome c oxidase dimers in triton X-100 and phospholipid vesicles by chemical cross-linking Biochemistry 32 1993 13270 13276
    • (1993) Biochemistry , vol.32 , pp. 13270-13276
    • Estey, L.1    Prochaska, L.J.2
  • 25
    • 0035823541 scopus 로고    scopus 로고
    • Exposure of bovine cytochrome c oxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F
    • R.C. Sadoski, D. Zaslavsky, R.B. Gennis, B. Durham, and F. Millet Exposure of bovine cytochrome c oxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F J. Biol. Chem. 276 2001 33616 33620
    • (2001) J. Biol. Chem. , vol.276 , pp. 33616-33620
    • Sadoski, R.C.1    Zaslavsky, D.2    Gennis, R.B.3    Durham, B.4    Millet, F.5
  • 26
    • 0022550464 scopus 로고
    • Characterization of electron transfer and proton translocation activities in bovine heart mitochondrial cytochrome c oxidase deficient in subunit III
    • L.J. Prochaska, and K.A. Reynolds Characterization of electron transfer and proton translocation activities in bovine heart mitochondrial cytochrome c oxidase deficient in subunit III Biochemistry 25 1986 781 787
    • (1986) Biochemistry , vol.25 , pp. 781-787
    • Prochaska, L.J.1    Reynolds, K.A.2
  • 30
    • 23544450428 scopus 로고
    • The extinction coefficient of cytochrome c
    • B.F. Van Gelder, and E.C. Slater The extinction coefficient of cytochrome c Biochim. Acta 58 1962 593 595
    • (1962) Biochim. Acta , vol.58 , pp. 593-595
    • Van Gelder, B.F.1    Slater, E.C.2
  • 31
    • 0015222174 scopus 로고
    • Studies on ferricytochrome c: 1. Effect of pH, ionic strength, and denaturants on the spectra of ferricytochrome c
    • C. Greenwood, and M.T. Wilson Studies on ferricytochrome c: 1. Effect of pH, ionic strength, and denaturants on the spectra of ferricytochrome c Eur. J. Biochem. 22 1971 5 10
    • (1971) Eur. J. Biochem. , vol.22 , pp. 5-10
    • Greenwood, C.1    Wilson, M.T.2
  • 33
    • 0018264560 scopus 로고
    • Definition of cytochrome c binding domains by chemical modification
    • S. Ferguson-Miller, D.L. Brautigan, and E. Margoliash Definition of cytochrome c binding domains by chemical modification J. Biol. Chem. 253 1978 149 159
    • (1978) J. Biol. Chem. , vol.253 , pp. 149-159
    • Ferguson-Miller, S.1    Brautigan, D.L.2    Margoliash, E.3
  • 34
    • 0942290629 scopus 로고    scopus 로고
    • Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide
    • A. Musatov, E. Hebert, C.A. Carroll, S.T. Weintraub, and N.C. Robinson Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide Biochemistry 43 2004 1003 1009
    • (2004) Biochemistry , vol.43 , pp. 1003-1009
    • Musatov, A.1    Hebert, E.2    Carroll, C.A.3    Weintraub, S.T.4    Robinson, N.C.5
  • 35
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • M.I. Verkhovsky, J.E. Morgan, and M. Wikstrom Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons Biochemistry 34 1995 7483 7491
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikstrom, M.3
  • 36
    • 0037092060 scopus 로고    scopus 로고
    • Detergent modulation of electron and proton transfer reactions in bovine cytochrome c oxidase
    • M. Tarasev, and B.C. Hill Detergent modulation of electron and proton transfer reactions in bovine cytochrome c oxidase Arch. Biochem. Biophys. 400 2002 162 170
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 162-170
    • Tarasev, M.1    Hill, B.C.2
  • 37
    • 0023711148 scopus 로고
    • Subunit dissociation and protein unfolding in the bovine heart cytochrome oxidase complex induced by guanidine hydrochloride
    • B.C. Hill, K. Cook, and N.C. Robinson Subunit dissociation and protein unfolding in the bovine heart cytochrome oxidase complex induced by guanidine hydrochloride Biochemistry 27 1988 4741 4747
    • (1988) Biochemistry , vol.27 , pp. 4741-4747
    • Hill, B.C.1    Cook, K.2    Robinson, N.C.3
  • 38
    • 0017340325 scopus 로고
    • Molecular architechture of cytochrome oxidase and its transition on treatment with alkali or sodium dodecyl sulfate
    • Y. Orii, M. Manabe, and M. Yoneda Molecular architechture of cytochrome oxidase and its transition on treatment with alkali or sodium dodecyl sulfate J. Biochem. 81 1977 505 517
    • (1977) J. Biochem. , vol.81 , pp. 505-517
    • Orii, Y.1    Manabe, M.2    Yoneda, M.3
  • 39
    • 0029122404 scopus 로고
    • Cytochrome c oxidase: Biphasic kinetics result from incomplete reduction of cytochrome a by cytochrome c bound to the high affinity site
    • J. Ortega-Lopez, and N.C. Robinson Cytochrome c oxidase: biphasic kinetics result from incomplete reduction of cytochrome a by cytochrome c bound to the high affinity site Biochemistry 34 1995 10000 10008
    • (1995) Biochemistry , vol.34 , pp. 10000-10008
    • Ortega-Lopez, J.1    Robinson, N.C.2
  • 40
    • 0025061009 scopus 로고
    • Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electron transfer steps
    • S.N. Mahapatro, and N.C. Robinson Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electron transfer steps Biochemistry 29 1990 764 770
    • (1990) Biochemistry , vol.29 , pp. 764-770
    • Mahapatro, S.N.1    Robinson, N.C.2
  • 41
    • 0021763113 scopus 로고
    • The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature
    • B.C. Hill, and C. Greenwood The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature Biochem. J. 218 1984 913 921
    • (1984) Biochem. J. , vol.218 , pp. 913-921
    • Hill, B.C.1    Greenwood, C.2
  • 44
    • 0021107158 scopus 로고
    • Origin of the cytochrome a absorption red-shift: A pH dependent interaction between its heme a formyl and protein in cytochrome oxidase
    • P.M. Callahan, and G.T. Babcock Origin of the cytochrome a absorption red-shift: a pH dependent interaction between its heme a formyl and protein in cytochrome oxidase Biochemistry 22 1983 452 461
    • (1983) Biochemistry , vol.22 , pp. 452-461
    • Callahan, P.M.1    Babcock, G.T.2
  • 45
    • 0016162084 scopus 로고
    • Biochemical and biophysical studies on cytochrome c oxidase: XVIII. Potentiometric titrations of cytochrome c oxidase followed by circular dichroism
    • R.H. Tiesjma, G.P.M.A. Hardy, and B.F. Van Gelder Biochemical and biophysical studies on cytochrome c oxidase: XVIII. Potentiometric titrations of cytochrome c oxidase followed by circular dichroism Biochim. Biophys. Acta 357 1974 24 33
    • (1974) Biochim. Biophys. Acta , vol.357 , pp. 24-33
    • Tiesjma, R.H.1    Hardy, G.P.M.A.2    Van Gelder, B.F.3
  • 46
    • 0025008307 scopus 로고
    • Chemical labeling studies on bovine heart mitochondrial cytochrome c oxidase dispersed in nonionic detergents
    • L.A. Estey, A.J. Lincoln, and L.J. Prochaska Chemical labeling studies on bovine heart mitochondrial cytochrome c oxidase dispersed in nonionic detergents Biochemistry 29 1990 9714 9720
    • (1990) Biochemistry , vol.29 , pp. 9714-9720
    • Estey, L.A.1    Lincoln, A.J.2    Prochaska, L.J.3
  • 47
    • 0030451817 scopus 로고    scopus 로고
    • Physical and functional characterisation of monomeric and dimeric eukaryotic cytochrome c oxidases
    • C. Blenkinsop, A.E. Aitken, and M.T. Wilson Physical and functional characterisation of monomeric and dimeric eukaryotic cytochrome c oxidases Comp. Biochem. Physiol. 115B 1996 421 428
    • (1996) Comp. Biochem. Physiol. , vol.115 , pp. 421-428
    • Blenkinsop, C.1    Aitken, A.E.2    Wilson, M.T.3
  • 48
    • 0026064432 scopus 로고
    • A of cytochrome c oxidase in intact liver mitochondria
    • A of cytochrome c oxidase in intact liver mitochondria Biochemistry 30 1991 948 956
    • (1991) Biochemistry , vol.30 , pp. 948-956
    • Morgan, J.E.1    Wikstrom, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.