메뉴 건너뛰기




Volumn 51, Issue 34, 2012, Pages 6804-6815

Human sulfide:Quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON ACCEPTOR; HEALTHY INDIVIDUALS; HYDROGEN SULFIDE METABOLISM; LOW TEMPERATURES; MAMMALIAN TISSUES; MEMBRANE-BOUND ENZYMES; MITOCHONDRIAL METABOLISM; OXIDOREDUCTASES; PATHOLOGICAL CONDITIONS; PH OPTIMA; PHYSIOLOGICAL PH; PROSTHETIC GROUPS; SULFUR ANALOGUES; SYNTHETIC GENES; TWO-ELECTRON OXIDATION;

EID: 84867522886     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300778t     Document Type: Article
Times cited : (232)

References (63)
  • 2
    • 0022464168 scopus 로고
    • Metabolism of sulfur-containing amino acids
    • Stipanuk, M. H. (1986) Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 6, 179-209.
    • (1986) Annu. Rev. Nutr , vol.6 , pp. 179-209
    • Stipanuk, M.H.1
  • 3
    • 0036700930 scopus 로고    scopus 로고
    • Hydrogen sulfide as a neuromodulator
    • Kimura, H. (2002) Hydrogen sulfide as a neuromodulator. Mol. Neurobiol. 26, 13-19.
    • (2002) Mol. Neurobiol , vol.26 , pp. 13-19
    • Kimura, H.1
  • 4
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura, Y., and Kimura, H. (2004) Hydrogen sulfide protects neurons from oxidative stress. FASEB J. 18, 1165-1167.
    • (2004) FASEB J , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 5
    • 73449101844 scopus 로고    scopus 로고
    • Hydrogen sulfide-releasing nsaids attenuate neuroinflammation induced by microglial and astrocytic activation
    • Lee, M., Sparatore, A., Del Soldato, P., Mcgeer, E., and McGeer, P. L. (2010) Hydrogen sulfide-releasing NSAIDs attenuate neuroinflammation induced by microglial and astrocytic activation. Glia 58, 103-113.
    • (2010) Glia , vol.58 , pp. 103-113
    • Lee, M.1    Sparatore, A.2    Del Soldato, P.3    Mcgeer, E.4    McGeer, P.L.5
  • 6
    • 78650541124 scopus 로고    scopus 로고
    • Hydrogen sulfidemediated myocardial pre-And post-conditioning
    • Predmore, B. L., and Lefer, D. J. (2011) Hydrogen sulfidemediated myocardial pre-And post-conditioning. Expert Rev. Clin. Pharmacol. 4, 83.
    • (2011) Expert Rev. Clin. Pharmacol , vol.4 , pp. 83
    • Predmore, B.L.1    Lefer, D.J.2
  • 8
    • 54949084607 scopus 로고    scopus 로고
    • H2s as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine γ-lyase
    • Yang, G., Wu, L., Jiang, B., Yang, W., Qi, J., Cao, K., Meng, Q., Mustafa, A. K., Mu, W., and Zhang, S. (2008) H2S as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine γ-lyase. Science 322, 587-590.
    • (2008) Science , vol.322 , pp. 587-590
    • Yang, G.1    Wu, L.2    Jiang, B.3    Yang, W.4    Qi, J.5    Cao, K.6    Meng, Q.7    Mustafa, A.K.8    Mu, W.9    Zhang, S.10
  • 10
    • 20244390001 scopus 로고    scopus 로고
    • H2s induces a suspended animation-like state in mice
    • Blackstone, E., Morrison, M., and Roth, M. B. (2005) H2S induces a suspended animation-like state in mice. Science 308, 518.
    • (2005) Science , vol.308 , pp. 518
    • Blackstone, E.1    Morrison, M.2    Roth, M.B.3
  • 14
    • 84862909327 scopus 로고    scopus 로고
    • Hydrogen sulfide-linked sulfhydration of nf-κb mediates its antiapoptotic actions
    • Sen, N., Paul, B. D., Gadalla, M. M., Mustafa, A. K., Sen, T., Xu, R., Kim, S., and Snyder, S. H. (2012) Hydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actions. Mol. Cell 45, 13-24.
    • (2012) Mol. Cell , vol.45 , pp. 13-24
    • Sen, N.1    Paul, B.D.2    Gadalla, M.M.3    Mustafa, A.K.4    Sen, T.5    Xu, R.6    Kim, S.7    Snyder, S.H.8
  • 16
    • 83655165310 scopus 로고    scopus 로고
    • H2s-induced sulfhydration of the phosphatase ptp1b and its role in the endoplasmic reticulum stress response
    • Krishnan, N., Fu, C. X., Pappin, D. J., and Tonks, N. K. (2011) H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress Response. Sci. Signal 4, ra86.
    • (2011) Sci. Signal , vol.4
    • Krishnan, N.1    Fu, C.X.2    Pappin, D.J.3    Tonks, N.K.4
  • 17
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil, O., and Banerjee, R. (2010) Redox biochemistry of hydrogen sulfide. J. Biol. Chem. 285, 21903-21907.
    • (2010) J. Biol. Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 18
    • 0035030625 scopus 로고    scopus 로고
    • Sulfide oxidation coupled to atp synthesis in chicken liver mitochondria
    • Yong, R., and Searcy, D. G. (2001) Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 129, 129-137.
    • (2001) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol , vol.129 , pp. 129-137
    • Yong, R.1    Searcy, D.G.2
  • 19
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
    • Hildebrandt, T. M., and Grieshaber, M. F. (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J. 275, 3352-3361.
    • (2008) FEBS J , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.F.2
  • 20
    • 0010494571 scopus 로고    scopus 로고
    • Biological sulfide oxidation: Sulfide-quinone reductase (sqr), the primary reaction
    • (Pandalai, S. G., Ed.), Research Signpost, Trivandrum, India
    • Griesbeck, C., Hauska, G., and Schütz, M. (2000) Biological sulfide oxidation: Sulfide-quinone reductase (SQR), the primary reaction. In Recent Research Developments in Microbiology (Pandalai, S. G., Ed.) pp 179-203, Research Signpost, Trivandrum, India.
    • (2000) Recent Research Developments in Microbiology , pp. 179-203
    • Griesbeck, C.1    Hauska, G.2    Schütz, M.3
  • 21
    • 64149124736 scopus 로고    scopus 로고
    • Sulfide oxidation from cyanobacteria to humans: Sulfide-quinone oxidoreductase (sqr
    • (Hell, R., Dahl, C., Knaff, D. B., and Leustek, T., Eds.), Springer, Heidelberg, Germany
    • Shahak, Y., and Hauska, G. (2008) Sulfide oxidation from cyanobacteria to humans: Sulfide-quinone oxidoreductase (SQR). In Advances in photosynthesis and respiration (Hell, R., Dahl, C., Knaff, D. B., and Leustek, T., Eds.) pp 320-335, Springer, Heidelberg, Germany.
    • (2008) Advances in Photosynthesis and Respiration , pp. 320-335
    • Shahak, Y.1    Hauska, G.2
  • 22
    • 40349111259 scopus 로고    scopus 로고
    • Sulfide:quinone oxidoreductase from the lugworm arenicola marina shows cyanideand thioredoxin-dependent activity
    • Theissen, U., and Martin, W. (2008) Sulfide:quinone oxidoreductase from the lugworm Arenicola marina shows cyanideand thioredoxin-dependent activity. FEBS J. 275, 1131-1139.
    • (2008) FEBS J , vol.275 , pp. 1131-1139
    • Theissen, U.1    Martin, W.2
  • 23
    • 77951225834 scopus 로고    scopus 로고
    • A new structure-based classification of sulfide:quinone oxidoreductases
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2010) A new structure-based classification of sulfide:quinone oxidoreductases. Proteins 78, 1073-1083.
    • (2010) Proteins , vol.78 , pp. 1073-1083
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 24
    • 0033532082 scopus 로고    scopus 로고
    • A fission yeast gene for mitochondrial sulfide oxidation
    • Weghe, J. G. V., and Ow, D. W. (1999) A fission yeast gene for mitochondrial sulfide oxidation. J. Biol. Chem. 274, 13250-13257.
    • (1999) J. Biol. Chem , vol.274 , pp. 13250-13257
    • Weghe, J.G.V.1    Ow, D.W.2
  • 25
    • 67649872642 scopus 로고    scopus 로고
    • The structure of aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2009) The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc. Natl. Acad. Sci. U.S.A. 106, 9625-9630.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 27
    • 77951703678 scopus 로고    scopus 로고
    • Crystal structure of sulfide:quinone oxidoreductase from acidithiobacillus ferrooxidans: Insights into sulfidotrophic respiration and detoxification
    • Cherney, M. M., Zhang, Y. F., Solomonson, M., Weiner, J. H., and James, M. N. G. (2010) Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: Insights into sulfidotrophic respiration and detoxification. J. Mol. Biol. 398, 292-305.
    • (2010) J. Mol. Biol , vol.398 , pp. 292-305
    • Cherney, M.M.1    Zhang, Y.F.2    Solomonson, M.3    Weiner, J.H.4    James, M.N.G.5
  • 28
    • 0022974540 scopus 로고
    • Bacterial sarcosine oxidase: Comparison of two multisubunit enzymes containing both covalent and noncovalent flavin
    • Kvalnes-Krick, K., and Jorns, M. S. (1986) Bacterial sarcosine oxidase: Comparison of two multisubunit enzymes containing both covalent and noncovalent flavin. Biochemistry 25, 6061-6069.
    • (1986) Biochemistry , vol.25 , pp. 6061-6069
    • Kvalnes-Krick, K.1    Jorns, M.S.2
  • 29
    • 0033609040 scopus 로고    scopus 로고
    • Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and n-methyltryptophan oxidase
    • Wagner, M. A., Khanna, P., and Jorns, M. S. (1999) Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and N-methyltryptophan oxidase. Biochemistry 38, 5588-5595.
    • (1999) Biochemistry , vol.38 , pp. 5588-5595
    • Wagner, M.A.1    Khanna, P.2    Jorns, M.S.3
  • 30
    • 70350018323 scopus 로고    scopus 로고
    • Making and working with hydrogen sulfide: The chemistry and generation of hydrogen sulfide in vitro and its measurement in vivo: A review
    • Hughes, M. N., Centelles, M. N., and Moore, K. P. (2009) Making and working with hydrogen sulfide: The chemistry and generation of hydrogen sulfide in vitro and its measurement in vivo: A review. Free Radical Biol. Med. 47, 1346-1353.
    • (2009) Free Radical Biol. Med , vol.47 , pp. 1346-1353
    • Hughes, M.N.1    Centelles, M.N.2    Moore, K.P.3
  • 31
    • 0019644226 scopus 로고
    • Spectroscopic properties of ubiquinones in model systems
    • Esposti, D. M., Ferri, E., and Lenaz, G. (1981) Spectroscopic properties of ubiquinones in model systems. Ital. J. Biochem. 30, 437-452.
    • (1981) Ital. J. Biochem , vol.30 , pp. 437-452
    • Esposti, D.M.1    Ferri, E.2    Lenaz, G.3
  • 32
    • 0000196317 scopus 로고
    • A colorimetric method for the determination of thiosulfate
    • Sorbo, B. (1957) A colorimetric method for the determination of thiosulfate. Biochim. Biophys. Acta 23, 412-416.
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 412-416
    • Sorbo, B.1
  • 33
    • 0023070121 scopus 로고
    • Sulfane sulfur
    • Wood, J. L. (1987) Sulfane sulfur. Methods Enzymol. 143, 25-29.
    • (1987) Methods Enzymol , vol.143 , pp. 25-29
    • Wood, J.L.1
  • 35
    • 0028068353 scopus 로고
    • Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity
    • Kessi, J., Poirée, J. C., Wehrli, E., Bachofen, R., Semenza, G., and Hauser, H. (1994) Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity. Biochemistry 33, 10825-10836.
    • (1994) Biochemistry , vol.33 , pp. 10825-10836
    • Kessi, J.1    Poirée, J.2    Wehrli, E.3    Bachofen, R.4    Semenza, G.5    Hauser, H.6
  • 36
    • 84981833621 scopus 로고
    • Der acidität der sulfane and die zusammensetzung wässeriger polysulfidlösungen
    • Schwarzenbach, G., and Fischer, A. (1960) Der Acidität der Sulfane and die Zusammensetzung wässeriger Polysulfidlösungen. Helv. Chim. Acta 43, 1365-1390.
    • (1960) Helv. Chim. Acta , vol.43 , pp. 1365-1390
    • Schwarzenbach, G.1    Fischer, A.2
  • 37
    • 27144526825 scopus 로고
    • Beiträge zur chemie des schwefels, 62. Ultraviolett- Absorptionsspektren kettenförmiger schwefelverbindungen
    • Fehér, F., and Münzner, H. (1963) Beiträge zur Chemie des Schwefels, 62. Ultraviolett-Absorptionsspektren kettenförmiger Schwefelverbindungen. Z. Anorg. Allg. Chem. 96, 1131-1149.
    • (1963) Z. Anorg. Allg. Chem , vol.96 , pp. 1131-1149
    • Fehér, F.1    Münzner, H.2
  • 38
    • 0001655308 scopus 로고
    • Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20°
    • Giggenbach, W. (1972) Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20°. Inorg. Chem. 11, 1201-1207.
    • (1972) Inorg. Chem , vol.11 , pp. 1201-1207
    • Giggenbach, W.1
  • 39
    • 0014691135 scopus 로고
    • Metabolic interrelations of sulfur in proteins, thiosulfate, and cystine
    • Schneider, J. F., and Westley, J. (1969) Metabolic interrelations of sulfur in proteins, thiosulfate, and cystine. J. Biol. Chem. 244, 5735.
    • (1969) J. Biol. Chem , vol.244 , pp. 5735
    • Schneider, J.F.1    Westley, J.2
  • 40
    • 64049098303 scopus 로고    scopus 로고
    • Regulation of active site coupling in glutamine-dependent nad+ synthetase
    • LaRonde-LeBlanc, N., Resto, M., and Gerratana, B. (2009) Regulation of active site coupling in glutamine-dependent NAD+ synthetase. Nat. Struct. Mol. Biol. 16, 421-429.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 421-429
    • LaRonde-LeBlanc, N.1    Resto, M.2    Gerratana, B.3
  • 42
    • 0002767481 scopus 로고
    • The enzymatic synthesis of d-Alanyl-dalanine. I. Kinetic studies on d-Alanyl-d-Alanine synthetase
    • Neuhaus, F. C. (1962) The enzymatic synthesis of D-Alanyl-Dalanine. I. Kinetic studies on D-Alanyl-D-Alanine synthetase. J. Biol. Chem. 237, 3128-3135.
    • (1962) J. Biol. Chem , vol.237 , pp. 3128-3135
    • Neuhaus, F.C.1
  • 44
    • 0032478595 scopus 로고    scopus 로고
    • The glutathione dependence of inorganic sulfate formation from l-or d-cysteine in isolated rat hepatocytes
    • Huang, J., Khan, S., and O'Brien, P. J. (1998) The glutathione dependence of inorganic sulfate formation from L-or D-cysteine in isolated rat hepatocytes. Chem.-Biol. Interact. 110, 189-202.
    • (1998) Chem.-Biol. Interact , vol.110 , pp. 189-202
    • Huang, J.1    Khan, S.2    O'Brien, P.J.3
  • 45
    • 0032718594 scopus 로고    scopus 로고
    • Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa
    • Levitt, M. D., Furne, J., Springfield, J., Suarez, F., and DeMaster, E. (1999) Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa. J. Clin. Invest. 104, 1107-1114.
    • (1999) J. Clin. Invest , vol.104 , pp. 1107-1114
    • Levitt, M.D.1    Furne, J.2    Springfield, J.3    Suarez, F.4    DeMaster, E.5
  • 46
    • 0014178501 scopus 로고
    • Oxidation of thiosulphate to sulphate in animal tissues
    • Koj, A., and Frendo, J. (1967) Oxidation of thiosulphate to sulphate in animal tissues. Folia Biol. (Krakow, Pol.) 15, 49-65.
    • (1967) Folia Biol. (Krakow, Pol , vol.15 , pp. 49-65
    • Koj, A.1    Frendo, J.2
  • 47
    • 0032568532 scopus 로고    scopus 로고
    • Human sulfite oxidase r160q: Identification of the mutation in a sulfide oxidase-deficient patient and expression and characterization of the mutant enzyme
    • Garrett, R. M., Johnson, J. L., Graf, T. N., Feigenbaum, A., and Rajagopalan, K. V. (1998) Human sulfite oxidase R160Q: Identification of the mutation in a sulfide oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc. Natl. Acad. Sci. U.S.A. 95, 6394-6398.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 6394-6398
    • Garrett, R.M.1    Johnson, J.L.2    Graf, T.N.3    Feigenbaum, A.4    Rajagopalan, K.V.5
  • 48
    • 0014098318 scopus 로고
    • 35S Thiosulphate oxidation by rat liver mitochondria in the presence of glutathione
    • Koj, A., Frendo, J., and Janik, Z. (1967) [35S]Thiosulphate oxidation by rat liver mitochondria in the presence of glutathione. Biochem. J. 103, 791.
    • (1967) Biochem. J , vol.103 , pp. 791
    • Koj, A.1    Frendo, J.2    Janik, Z.3
  • 49
    • 0344963392 scopus 로고
    • The metabolic state of thiosulfate
    • Szczepkowski, T. W., Skarzynski, B., and Weber, M. (1961) The metabolic state of thiosulfate. Nature 189, 1007-1008.
    • (1961) Nature , vol.189 , pp. 1007-1008
    • Szczepkowski, T.W.1    Skarzynski, B.2    Weber, M.3
  • 50
    • 0016722749 scopus 로고
    • The catalytic mechanism of carbonic anhydrase
    • Steiner, H., Jonsson, B. H., and Lindskog, S. (1975) The catalytic mechanism of carbonic anhydrase. Eur. J. Biochem. 59, 253-259.
    • (1975) Eur. J. Biochem , vol.59 , pp. 253-259
    • Steiner, H.1    Jonsson, B.H.2    Lindskog, S.3
  • 51
    • 77957011016 scopus 로고
    • Rhodanese
    • Sorbo, B. H. (1955) Rhodanese. Methods Enzymol. 2, 334-337.
    • (1955) Methods Enzymol , vol.2 , pp. 334-337
    • Sorbo, B.H.1
  • 52
    • 84858195283 scopus 로고    scopus 로고
    • Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the cns
    • Linden, D. R., Furne, J., Stoltz, G. J., Abdel-Rehim, M. S., Levitt, M. D., and Szurszewski, J. H. (2012) Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the CNS. Br. J. Pharmacol. 165, 2178-2190.
    • (2012) Br. J. Pharmacol , vol.165 , pp. 2178-2190
    • Linden, D.R.1    Furne, J.2    Stoltz, G.J.3    Abdel-Rehim, M.S.4    Levitt, M.D.5    Szurszewski, J.H.6
  • 54
    • 76749087089 scopus 로고    scopus 로고
    • Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase
    • Johnson-Winters, K., Nordstrom, A. R., Emesh, S., Astashkin, A. V., Rajapakshe, A., Berry, R. E., Tollin, G., and Enemark, J. H. (2010) Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase. Biochemistry 49, 1290-1296.
    • (2010) Biochemistry , vol.49 , pp. 1290-1296
    • Johnson-Winters, K.1    Nordstrom, A.R.2    Emesh, S.3    Astashkin, A.V.4    Rajapakshe, A.5    Berry, R.E.6    Tollin, G.7    Enemark, J.H.8
  • 56
    • 0023196348 scopus 로고
    • Urinary thiosulphate as an indicator of exposure to hydrogen sulphide vapour
    • Kangas, J., and Savolainen, H. (1987) Urinary thiosulphate as an indicator of exposure to hydrogen sulphide vapour. Clin. Chim. Acta 164, 7-10.
    • (1987) Clin. Chim. Acta , vol.164 , pp. 7-10
    • Kangas, J.1    Savolainen, H.2
  • 58
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathioine reductase, thioredoxin reductase, and mercuric ion reductase: A family of flavoenzyme transhydrogenases
    • (Muller, F., Ed.), CRC Press, Boca Raton, FL
    • Williams, C. H. (1992) Lipoamide dehydrogenase, glutathioine reductase, thioredoxin reductase, and mercuric ion reductase: A family of flavoenzyme transhydrogenases. In Chemistry and Biochemistry of Flavoenzymes (Muller, F., Ed.) Vol. III, pp 121-211, CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 121-211
    • Williams, C.H.1
  • 60
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-coa dehydrogenases: A mechanistic overview
    • Ghisla, S., and Thorpe, C. (2004) Acyl-CoA dehydrogenases: A mechanistic overview. Eur. J. Biochem. 271, 494-508.
    • (2004) Eur. J. Biochem , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 61
    • 0034254540 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants
    • Wagner, M. A., Trickey, P., Chen, Z., Mathews, F. S., and Jorns, M. S. (2000) Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants. Biochemistry 39, 8813-8824.
    • (2000) Biochemistry , vol.39 , pp. 8813-8824
    • Wagner, M.A.1    Trickey, P.2    Chen, Z.3    Mathews, F.S.4    Jorns, M.S.5
  • 62
    • 0022393945 scopus 로고
    • Potentionmetric studies of native and flavin-substituted old yellow enzyme
    • Steward, R. C., and Massey, V. (1985) Potentionmetric studies of native and flavin-substituted old yellow enzyme. J. Biol. Chem. 260, 13639-13647.
    • (1985) J. Biol. Chem , vol.260 , pp. 13639-13647
    • Steward, R.C.1    Massey, V.2
  • 63
    • 0020490576 scopus 로고
    • Evidence that the greening ligand in native butyryl-coa dehydrogenase is a coa persulfide
    • Williamson, G., Engel, P. C., Mizzer, J. P., Thorpe, C., and Massey, V. (1982) Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide. J. Biol. Chem. 257, 4314-4320.
    • (1982) J. Biol. Chem , vol.257 , pp. 4314-4320
    • Williamson, G.1    Engel, P.C.2    Mizzer, J.P.3    Thorpe, C.4    Massey, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.