메뉴 건너뛰기




Volumn 80, Issue 2, 2012, Pages 546-555

A temperature-dependent conformational change of NADH oxidase from Thermus thermophilus HB8

Author keywords

Electron transfer; Flavoproteins; Fluorescence; Fluorescence quenching; Molecular dynamics; NADH oxidase; Temperature effects; Thermophiles; Thermophilic enzymes; Thermus thermophilus

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TRYPTOPHAN; MULTIENZYME COMPLEX; OXIDOREDUCTASE; TYROSINE;

EID: 84855663873     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23219     Document Type: Article
Times cited : (7)

References (46)
  • 1
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 2001; 65: 1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 2
    • 0025822794 scopus 로고
    • Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinase from yeast and Thermus thermophilus
    • Varley PG, Pain RH. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinase from yeast and Thermus thermophilus. J Mol Biol 1991; 220: 531-538.
    • (1991) J Mol Biol , vol.220 , pp. 531-538
    • Varley, P.G.1    Pain, R.H.2
  • 3
    • 0027587611 scopus 로고
    • Purification and characterization of a highly stable glucose isomerase produced by the extremely thermophilic eubacterium, Thermotoga maritima
    • Brown SH, Sjolholm C, Kelley RM. Purification and characterization of a highly stable glucose isomerase produced by the extremely thermophilic eubacterium, Thermotoga maritima. Biotechnol Bioeng 1993; 41: 878-886.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 878-886
    • Brown, S.H.1    Sjolholm, C.2    Kelley, R.M.3
  • 6
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur J Biochem 1991; 202: 715-728.
    • (1991) Eur J Biochem , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 7
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Böhm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998; 8: 738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 8
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen M. Relationship of protein flexibility to thermostability. Protein Eng 1987; 1: 477-480.
    • (1987) Protein Eng , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 9
    • 0002353040 scopus 로고
    • Temperature adaptation of enzymes: biological optimization through structure-function compromises
    • Somero GN. Temperature adaptation of enzymes: biological optimization through structure-function compromises. Annu Rev Ecol Syst 1978; 9: 1-29.
    • (1978) Annu Rev Ecol Syst , vol.9 , pp. 1-29
    • Somero, G.N.1
  • 11
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba A, Schweiger A, Schultes V, Jaenicke R, Zavodsky P. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry (Moscow) 1990; 29: 7584-7592.
    • (1990) Biochemistry (Moscow) , vol.29 , pp. 7584-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodsky, P.5
  • 12
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodsky P, Kardos J, Svingor A, Petsko GA. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA 1998; 95: 7406-7411.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7406-7411
    • Zavodsky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 13
    • 0034327617 scopus 로고    scopus 로고
    • Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases
    • Kohen A, Klinman JP. Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases. J Am Chem Soc 2000; 122: 10738-10739.
    • (2000) J Am Chem Soc , vol.122 , pp. 10738-10739
    • Kohen, A.1    Klinman, J.P.2
  • 14
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
    • Hernandez G, Jenney FE, Adams MWW, LeMaster DM. Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc Natl Acad Sci USA 2000; 97: 3166-3170.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney, F.E.2    Adams, M.W.W.3    LeMaster, D.M.4
  • 15
    • 45849083521 scopus 로고    scopus 로고
    • Protein dynamics and stability: the distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering
    • Meinhold L, Clement D, Tehei M, Daniel R, Finney JL, Smith JC. Protein dynamics and stability: the distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering. Biophys J 2008; 94: 4812-4818.
    • (2008) Biophys J , vol.94 , pp. 4812-4818
    • Meinhold, L.1    Clement, D.2    Tehei, M.3    Daniel, R.4    Finney, J.L.5    Smith, J.C.6
  • 16
    • 77951143923 scopus 로고    scopus 로고
    • Temperature dependence of the flexibility of thermophilic and mesophilic members of the nitroreductase fold family
    • Merkley ED, Parson WW, Daggett V. Temperature dependence of the flexibility of thermophilic and mesophilic members of the nitroreductase fold family. Prot Eng Des Sel 2010; 23: 327-336.
    • (2010) Prot Eng Des Sel , vol.23 , pp. 327-336
    • Merkley, E.D.1    Parson, W.W.2    Daggett, V.3
  • 17
    • 0026525312 scopus 로고
    • Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus Hb8
    • Park HJ, Reiser COA, Kondruweit S, Erdmann H, Schmid RD, Sprinzl M. Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus Hb8. Eur J Biochem 1992; 205: 881-885.
    • (1992) Eur J Biochem , vol.205 , pp. 881-885
    • Park, H.J.1    Reiser, C.O.A.2    Kondruweit, S.3    Erdmann, H.4    Schmid, R.D.5    Sprinzl, M.6
  • 18
    • 28444436318 scopus 로고    scopus 로고
    • pH-induced changes in activity and conformation of NADH oxidase from Thermus thermophilus
    • Žoldák G, Musatov A, Stupak M, Sprinzo M, Sedlák E. pH-induced changes in activity and conformation of NADH oxidase from Thermus thermophilus. Gen Physiol Biophys 2005; 24: 279-298.
    • (2005) Gen Physiol Biophys , vol.24 , pp. 279-298
    • Žoldák, G.1    Musatov, A.2    Stupak, M.3    Sprinzo, M.4    Sedlák, E.5
  • 19
    • 1642540001 scopus 로고    scopus 로고
    • Modulation of activity of NADH oxidase from Thermus thermophilus through change in flexibility in the enzyme active site induced by Hofmeister series anions
    • Žoldák G, Sprinzl M, Sedlák E. Modulation of activity of NADH oxidase from Thermus thermophilus through change in flexibility in the enzyme active site induced by Hofmeister series anions. Eur J Biochem 2004; 271: 48-57.
    • (2004) Eur J Biochem , vol.271 , pp. 48-57
    • Žoldák, G.1    Sprinzl, M.2    Sedlák, E.3
  • 20
    • 41949130006 scopus 로고    scopus 로고
    • Flexibility and enzyme activity of NADH oxidase from Thermus thermophilus in the presence of monovalent cations of Hofmeister series
    • Toth K, Sedlák E, Sprinzl M, Žoldák G. Flexibility and enzyme activity of NADH oxidase from Thermus thermophilus in the presence of monovalent cations of Hofmeister series. Biochim Biophys Acta 2008; 1784: 789-795.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 789-795
    • Toth, K.1    Sedlák, E.2    Sprinzl, M.3    Žoldák, G.4
  • 21
    • 17444434923 scopus 로고    scopus 로고
    • Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus
    • Žoldák G, Šut'ák R, Antalik M, Sprinzl M, Sedlák E. Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus. Eur J Biochem 2003; 270: 4887-4897.
    • (2003) Eur J Biochem , vol.270 , pp. 4887-4897
    • Žoldák, G.1    Šut'ák, R.2    Antalik, M.3    Sprinzl, M.4    Sedlák, E.5
  • 22
    • 33745633058 scopus 로고    scopus 로고
    • Cofactor assisted gating mechanism in the active site of NADH oxidase from Thermus thermophilus
    • Hritz J, Žoldák G, Sedlák E. Cofactor assisted gating mechanism in the active site of NADH oxidase from Thermus thermophilus. Proteins Struct Funct Bioinform 2006; 64: 465-476.
    • (2006) Proteins Struct Funct Bioinform , vol.64 , pp. 465-476
    • Hritz, J.1    Žoldák, G.2    Sedlák, E.3
  • 24
    • 0029633167 scopus 로고
    • Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution
    • Levitt M, Hirshberg M, Sharon R, Daggett V. Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution. Comput Phys Commun 1995; 91: 215-231.
    • (1995) Comput Phys Commun , vol.91 , pp. 215-231
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Daggett, V.4
  • 25
    • 0000125216 scopus 로고    scopus 로고
    • Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution
    • Levitt M, Hirshberg M, Sharon R, Laidig K, Daggett V. Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution. J Phys Chem B 1997; 101: 5051-5056.
    • (1997) J Phys Chem B , vol.101 , pp. 5051-5056
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Laidig, K.4    Daggett, V.5
  • 26
    • 3342918929 scopus 로고    scopus 로고
    • Methods for molecular dynamics simulations of protein folding/unfolding in solution
    • Beck DAC, Daggett V. Methods for molecular dynamics simulations of protein folding/unfolding in solution. Methods 2004; 34: 112-120.
    • (2004) Methods , vol.34 , pp. 112-120
    • Beck, D.A.C.1    Daggett, V.2
  • 28
    • 0026514394 scopus 로고
    • 2-forming NADH oxidase from the extreme thermophilic Thermus thermophilus Hb8 and its expression in Escherichia coli
    • 2-forming NADH oxidase from the extreme thermophilic Thermus thermophilus Hb8 and its expression in Escherichia coli. Eur J Biochem 1992; 205: 875-879.
    • (1992) Eur J Biochem , vol.205 , pp. 875-879
    • Park, H.J.1    Kreutzer, R.2    Reiser, C.O.A.3    Sprinzl, M.4
  • 29
    • 0032156765 scopus 로고    scopus 로고
    • Set of secondary emission standards for calibration of the spectral responsivity in emission spectroscopy
    • Gardecki JA, Maroncelli M. Set of secondary emission standards for calibration of the spectral responsivity in emission spectroscopy. Appl Spectrosc 1998; 52: 1179-1189.
    • (1998) Appl Spectrosc , vol.52 , pp. 1179-1189
    • Gardecki, J.A.1    Maroncelli, M.2
  • 30
    • 84945799762 scopus 로고
    • Fluorescence quantum yields of tryptophan and tyrosine
    • Chen RF. Fluorescence quantum yields of tryptophan and tyrosine. Anal Lett 1967; 1: 35-42.
    • (1967) Anal Lett , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 32
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov.: a nonsporulating thermophilic bacterium from a Japanese thermal spa
    • Oshima T, Imahori K. Description of Thermus thermophilus (Yoshida and Oshima) comb. nov.: a nonsporulating thermophilic bacterium from a Japanese thermal spa. Int J Syst Bacteriol 1974; 24: 102-112.
    • (1974) Int J Syst Bacteriol , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2
  • 34
    • 0031953365 scopus 로고    scopus 로고
    • Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase
    • van den Berg PAW, van Hoek A, Walentas CD, Perham RN, Visser, AJWG. Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase. Biophys J 1998; 74: 2046-2058.
    • (1998) Biophys J , vol.74 , pp. 2046-2058
    • van den Berg, P.A.W.1    van Hoek, A.2    Walentas, C.D.3    Perham, R.N.4    Visser, A.J.W.G.5
  • 35
    • 0000784140 scopus 로고    scopus 로고
    • Ultrafast fluorescence quenching dynamics of flavin chromophores in protein nanospace
    • Mataga N, Chosrowjan H, Shibata T, Tanaka F. Ultrafast fluorescence quenching dynamics of flavin chromophores in protein nanospace. J Phys Chem B 1998; 102: 7081-7084.
    • (1998) J Phys Chem B , vol.102 , pp. 7081-7084
    • Mataga, N.1    Chosrowjan, H.2    Shibata, T.3    Tanaka, F.4
  • 36
    • 0034321054 scopus 로고    scopus 로고
    • Dynamics and mechanisms of ultrafast fluorescence quenching reactions of flavin chromophores in protein nanospace
    • Mataga N, Chosrowjan H, Shibata T, Tanaka F, Nishina Y, Shiga K. Dynamics and mechanisms of ultrafast fluorescence quenching reactions of flavin chromophores in protein nanospace. J Phys Chem B 2000; 104: 10667-10677.
    • (2000) J Phys Chem B , vol.104 , pp. 10667-10677
    • Mataga, N.1    Chosrowjan, H.2    Shibata, T.3    Tanaka, F.4    Nishina, Y.5    Shiga, K.6
  • 37
    • 0037026757 scopus 로고    scopus 로고
    • Femtosecond fluorescence dynamics of flavoproteins: comparative studies on flavodoxin, its site-directed mutants, and riboflavin binding protein regarding ultrafast electron transfer in protein nanospaces
    • Mataga N, Chosrowjan H, Tanaka F, Taniguchi S. Femtosecond fluorescence dynamics of flavoproteins: comparative studies on flavodoxin, its site-directed mutants, and riboflavin binding protein regarding ultrafast electron transfer in protein nanospaces. J Phys Chem 2002; 106: 8917-8920.
    • (2002) J Phys Chem , vol.106 , pp. 8917-8920
    • Mataga, N.1    Chosrowjan, H.2    Tanaka, F.3    Taniguchi, S.4
  • 39
    • 33745512491 scopus 로고    scopus 로고
    • Short range photoinduced electron transfer in proteins: QM-MM simulations of tryptophan and flavin fluorescence quenching in proteins
    • Callis PR, Liu TQ. Short range photoinduced electron transfer in proteins: QM-MM simulations of tryptophan and flavin fluorescence quenching in proteins. Chem Phys 2006; 326: 230-239.
    • (2006) Chem Phys , vol.326 , pp. 230-239
    • Callis, P.R.1    Liu, T.Q.2
  • 41
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • Page C, Moser CC, Chen XX, Dutton PL. Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 1999; 402: 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 42
    • 0035946957 scopus 로고    scopus 로고
    • The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 Å, 1.8 Å, and 2.4 Å resolution
    • Lovering AL, Hyde EI, Searle PF, White SA. The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 Å, 1.8 Å, and 2.4 Å resolution. J Mol Biol 2001; 309: 203-213.
    • (2001) J Mol Biol , vol.309 , pp. 203-213
    • Lovering, A.L.1    Hyde, E.I.2    Searle, P.F.3    White, S.A.4
  • 44
    • 33846381622 scopus 로고    scopus 로고
    • Direct observation of microscopic reversibility in single-molecule protein unfolding
    • Day R, Daggett V. Direct observation of microscopic reversibility in single-molecule protein unfolding. J Mol Biol 2007; 366: 677-686.
    • (2007) J Mol Biol , vol.366 , pp. 677-686
    • Day, R.1    Daggett, V.2
  • 45
    • 38349166890 scopus 로고    scopus 로고
    • m: molecular dynamics studies of the thermal pretransition of ribonuclease A
    • m: molecular dynamics studies of the thermal pretransition of ribonuclease A. Biochemistry 2008; 47: 880-892.
    • (2008) Biochemistry , vol.47 , pp. 880-892
    • Merkley, E.D.1    Bernard, B.2    Daggett, V.3
  • 46
    • 46849113841 scopus 로고    scopus 로고
    • Microscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomain
    • McCully ME, Beck DA, Daggett V. Microscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomain. Biochemistry 2008; 47: 7079-7089.
    • (2008) Biochemistry , vol.47 , pp. 7079-7089
    • McCully, M.E.1    Beck, D.A.2    Daggett, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.