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Volumn 96, Issue 5, 2012, Pages 1265-1273

Comparison of alkyl hydroperoxide reductase and two water-forming NADH oxidases from Bacillus cereus ATCC 14579

Author keywords

Alkyl hydroperoxide reductase; Anaerobic bacterium; NADH oxidase; Oxygen scavenger

Indexed keywords

ALKYL HYDROPEROXIDE; ANAEROBIC BACTERIUM; ANAEROBIC MICROORGANISMS; DEFENSE SYSTEM; DITHIOTHREITOL; NADH OXIDASE; NADH OXIDATION; OPERATIONAL STABILITY; OPTIMUM ACTIVITY; OXYGEN SCAVENGERS; THERMOTOLERANT; TOTAL TURNOVER;

EID: 84871102018     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-3919-1     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0030736766 scopus 로고    scopus 로고
    • Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase
    • Calzi ML, Poole LB (1997) Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase. Biochemistry 36(43): 13357-13364
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13357-13364
    • Calzi, M.L.1    Poole, L.B.2
  • 2
    • 77952276905 scopus 로고    scopus 로고
    • Comparative transcriptomic and phenotypic analysis of the responses of Bacillus cereus to various disinfectant treatments
    • Ceragioli M, Mols M, Moezelaar R, Ghelardi E, Senesi S, Abee T (2010) Comparative transcriptomic and phenotypic analysis of the responses of Bacillus cereus to various disinfectant treatments. Appl Environ Microbiol 76(10): 3352-3360
    • (2010) Appl Environ Microbiol , vol.76 , Issue.10 , pp. 3352-3360
    • Ceragioli, M.1    Mols, M.2    Moezelaar, R.3    Ghelardi, E.4    Senesi, S.5    Abee, T.6
  • 3
    • 0034958892 scopus 로고    scopus 로고
    • Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis
    • de Felipe FL, Hugenholtz J (2001) Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis. Int Dairy J 11(1-2): 37-44
    • (2001) Int Dairy J , vol.11 , Issue.1-2 , pp. 37-44
    • De Felipe, F.L.1    Hugenholtz, J.2
  • 4
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • Demple B, Amabilecuevas CF (1991) Redox redux: the control of oxidative stress responses. Cell 67(5): 837-839
    • (1991) Cell , vol.67 , Issue.5 , pp. 837-839
    • Demple, B.1    Amabilecuevas, C.F.2
  • 5
    • 67149131592 scopus 로고    scopus 로고
    • Phenotypic and transcriptomic analyses of mildly and severely salt-stressed Bacillus cereus ATCC 14579 Cells
    • den Besten HMW, Mols M, Moezelaar R, Zwietering MH, Abee T (2009) Phenotypic and transcriptomic analyses of mildly and severely salt-stressed Bacillus cereus ATCC 14579 Cells. Appl Environ Microbiol 75(12): 4111-4119
    • (2009) Appl Environ Microbiol , vol.75 , Issue.12 , pp. 4111-4119
    • Den Besten, H.M.W.1    Mols, M.2    Moezelaar, R.3    Zwietering, M.H.4    Abee, T.5
  • 6
    • 2442423017 scopus 로고    scopus 로고
    • Studies on NADH oxidase and alkyl hydroperoxide reductase produced by Porphyromonas gingivalis
    • Diaz PI, Zilm PS,Wasinger V, Corthals GL, Rogers AH (2004) Studies on NADH oxidase and alkyl hydroperoxide reductase produced by Porphyromonas gingivalis. Oral Microbiol Immunol 19 (3): 137-143
    • (2004) Oral Microbiol Immunol , vol.19 , Issue.3 , pp. 137-143
    • Diaz, P.I.1    Zilm, P.S.2    Wasinger, V.3    Corthals, G.L.4    Rogers, A.H.5
  • 7
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis HR, Poole LB (1997) Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 36(43): 13349-13356
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 8
    • 0037415359 scopus 로고    scopus 로고
    • NADH oxidase from Lactobacillus brevis: A new catalyst for the regeneration of NAD
    • Geueke B, Riebel B, Hummel W (2003) NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD. Enzyme Microb Technol 32(2): 205-211
    • (2003) Enzyme Microb Technol , vol.32 , Issue.2 , pp. 205-211
    • Geueke, B.1    Riebel, B.2    Hummel, W.3
  • 9
    • 0022588682 scopus 로고
    • Double-blind analysis of the relation between adult periodontitis and systemic host response to suspected periodontal pathogens
    • Gmur R, Hrodek K, Saxer UP, Guggenheim B (1986) Double-blind analysis of the relation between adult periodontitis and systemic host response to suspected periodontal pathogens. Infect Immun 52(3): 768-776
    • (1986) Infect Immun , vol.52 , Issue.3 , pp. 768-776
    • Gmur, R.1    Hrodek, K.2    Saxer, U.P.3    Guggenheim, B.4
  • 10
    • 0027442902 scopus 로고
    • Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
    • Higuchi M, Shimada M, Yamamoto Y, Hayashi T, Koga T, Kamio Y (1993) Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. J Gen Microbiol 139: 2343-2351
    • (1993) J Gen Microbiol , vol.139 , pp. 2343-2351
    • Higuchi, M.1    Shimada, M.2    Yamamoto, Y.3    Hayashi, T.4    Koga, T.5    Kamio, Y.6
  • 11
    • 0032871251 scopus 로고    scopus 로고
    • Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans
    • Higuchi M, Yamamoto Y, Poole LB, Shimada M, Sato Y, Takahashi N, Kamio Y (1999) Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans. J Bacteriol 181(19): 5940-5947
    • (1999) J Bacteriol , vol.181 , Issue.19 , pp. 5940-5947
    • Higuchi, M.1    Yamamoto, Y.2    Poole, L.B.3    Shimada, M.4    Sato, Y.5    Takahashi, N.6    Kamio, Y.7
  • 12
    • 0035985581 scopus 로고    scopus 로고
    • How oxygen damages microbes: Oxygen tolerance and obligate anaerobiosis
    • Academic, London
    • Imlay JA (2002) How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Advances in microbial physiology, vol 46. Academic, London, pp 111-153
    • (2002) Advances in Microbial Physiology , vol.46 , pp. 111-153
    • Imlay, J.A.1
  • 13
    • 4644234429 scopus 로고    scopus 로고
    • Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis
    • Jiang RR, Bommarius AS (2004) Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis. Tetrahedron- Asymmetry 15(18): 2939-2944
    • (2004) Tetrahedron- Asymmetry , vol.15 , Issue.18 , pp. 2939-2944
    • Jiang, R.R.1    Bommarius, A.S.2
  • 14
    • 20544438578 scopus 로고    scopus 로고
    • Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435
    • Jiang RR, Riebel BR, Bommarius AS (2005) Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435. Adv Synth Catal 347 (7-8): 1139-1146
    • (2005) Adv Synth Catal , vol.347 , Issue.7-8 , pp. 1139-1146
    • Jiang, R.R.1    Riebel, B.R.2    Bommarius, A.S.3
  • 15
    • 13544276421 scopus 로고    scopus 로고
    • Enzymatic properties of the membranebound NADH oxidase system in the aerobic respiratory chain of Bacillus cereus
    • Kim MS, Kim YJ (2004) Enzymatic properties of the membranebound NADH oxidase system in the aerobic respiratory chain of Bacillus cereus. J Biochem Mol Biol 37(6): 753-756
    • (2004) J Biochem Mol Biol , vol.37 , Issue.6 , pp. 753-756
    • Kim, M.S.1    Kim, Y.J.2
  • 16
    • 0021951979 scopus 로고
    • Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides
    • Koike K, Kobayashi T, Ito S, Saitoh M (1985) Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides. J Biochem 97(5): 1279-1288
    • (1985) J Biochem , vol.97 , Issue.5 , pp. 1279-1288
    • Koike, K.1    Kobayashi, T.2    Ito, S.3    Saitoh, M.4
  • 17
    • 33747497810 scopus 로고    scopus 로고
    • The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: Insights into the conversion of O2 into two water molecules by the flavoenzyme
    • Lountos GT, Jiang RR, Wellborn WB, Thaler TL, Bommarius AS, Orville AM (2006) The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O2 into two water molecules by the flavoenzyme. Biochemistry 45(32): 9648-9659
    • (2006) Biochemistry , vol.45 , Issue.32 , pp. 9648-9659
    • Lountos, G.T.1    Jiang, R.R.2    Wellborn, W.B.3    Thaler, T.L.4    Bommarius, A.S.5    Orville, A.M.6
  • 18
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey V (2000) The chemical and biological versatility of riboflavin. Biochem Soc Trans 28: 283-296
    • (2000) Biochem Soc Trans , vol.28 , pp. 283-296
    • Massey, V.1
  • 19
    • 0014027814 scopus 로고
    • A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide
    • Massey V, Curti B (1966) A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide. J Biol Chem 241 (14): 3417-3423
    • (1966) J Biol Chem , vol.241 , Issue.14 , pp. 3417-3423
    • Massey, V.1    Curti, B.2
  • 20
    • 77952278258 scopus 로고    scopus 로고
    • Analysis of acid-stressed Bacillus cereus reveals a major oxidative response and inactivation-associated radical formation
    • Mols M, van Kranenburg R, van Melis CCJ, Moezelaar R, Abee T (2010) Analysis of acid-stressed Bacillus cereus reveals a major oxidative response and inactivation-associated radical formation. Environ Microbiol 12(4): 873-885
    • (2010) Environ Microbiol , vol.12 , Issue.4 , pp. 873-885
    • Mols, M.1    Van Kranenburg, R.2    Van Melis, C.C.J.3    Moezelaar, R.4    Abee, T.5
  • 21
    • 0029843572 scopus 로고    scopus 로고
    • Reaction mechanism of Amphibacillus xylanus NADH oxidase alkyl hydroperoxide reductase flavoprotein
    • Niimura Y, Massey V (1996) Reaction mechanism of Amphibacillus xylanus NADH oxidase alkyl hydroperoxide reductase flavoprotein. J Biol Chem 271(48): 30459-30464
    • (1996) J Biol Chem , vol.271 , Issue.48 , pp. 30459-30464
    • Niimura, Y.1    Massey, V.2
  • 22
    • 4644257598 scopus 로고    scopus 로고
    • An enzymatic process to α-ketoglutarate from L-glutamate: The coupled system L-glutamate dehydrogenase/NADH oxidase
    • Odman P, Wellborn WB, Bommarius AS (2004) An enzymatic process to α-ketoglutarate from L-glutamate: the coupled system L-glutamate dehydrogenase/NADH oxidase. Tetrahedron Asymmetry 15 (18): 2933-2937
    • (2004) Tetrahedron Asymmetry , vol.15 , Issue.18 , pp. 2933-2937
    • Odman, P.1    Wellborn, W.B.2    Bommarius, A.S.3
  • 23
    • 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 (1992) Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8. Eur J Biochem 205(3): 881-885
    • (1992) Eur J Biochem , vol.205 , Issue.3 , 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
  • 24
    • 0042406617 scopus 로고    scopus 로고
    • Cofactor regeneration of NAD(+) from NADH: Novel water-forming NADH oxidases
    • Riebel BR, Gibbs PR, Wellborn WB, Bommarius AS (2002) Cofactor regeneration of NAD(+) from NADH: novel water-forming NADH oxidases. Adv Synth Catal 344(10): 1156-1168
    • (2002) Adv Synth Catal , vol.344 , Issue.10 , pp. 1156-1168
    • Riebel, B.R.1    Gibbs, P.R.2    Wellborn, W.B.3    Bommarius, A.S.4
  • 25
    • 0026795398 scopus 로고
    • Molecular-cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10 C1: Comparison with NADH peroxidase and the flavoprotein disulfide reductases
    • Ross RP, Claiborne A (1992) Molecular-cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10 C1: comparison with NADH peroxidase and the flavoprotein disulfide reductases. J Mol Biol 227(3): 658-671
    • (1992) J Mol Biol , vol.227 , Issue.3 , pp. 658-671
    • Ross, R.P.1    Claiborne, A.2
  • 26
    • 0022396889 scopus 로고
    • Purification and properties of NADH oxidase from Bacillus megaterium
    • Saeki Y, Nozaki M, Matsumoto K (1985) Purification and properties of NADH oxidase from Bacillus megaterium. J Biochem 98 (6): 1433-1440
    • (1985) J Biochem , vol.98 , Issue.6 , pp. 1433-1440
    • Saeki, Y.1    Nozaki, M.2    Matsumoto, K.3
  • 27
    • 0022558921 scopus 로고
    • Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis
    • Schmidt HL, Stocklein W, Danzer J, Kirch P, Limbach B (1986) Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis. Eur J Biochem 156(1): 149-155
    • (1986) Eur J Biochem , vol.156 , Issue.1 , pp. 149-155
    • Schmidt, H.L.1    Stocklein, W.2    Danzer, J.3    Kirch, P.4    Limbach, B.5
  • 28
    • 34447519155 scopus 로고    scopus 로고
    • Two distinct manganese-containing superoxide dismutase genes in Bacillus cereus: Their physiological characterizations and roles in surviving in wheat rhizosphere
    • Wang YJ, Wang HM, Yang CH, Wang Q, Mei RH (2007) Two distinct manganese-containing superoxide dismutase genes in Bacillus cereus: their physiological characterizations and roles in surviving in wheat rhizosphere. FEMS Microbiol Lett 272(2): 206-213
    • (2007) FEMS Microbiol Lett , vol.272 , Issue.2 , pp. 206-213
    • Wang, Y.J.1    Wang, H.M.2    Yang, C.H.3    Wang, Q.4    Mei, R.H.5
  • 29
    • 77957328836 scopus 로고    scopus 로고
    • Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes
    • Wang L, Wei L, Chen Y, Jiang RR (2010) Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes. J Biotechnol 150(1): 57-63
    • (2010) J Biotechnol , vol.150 , Issue.1 , pp. 57-63
    • Wang, L.1    Wei, L.2    Chen, Y.3    Jiang, R.R.4
  • 30
    • 84855219549 scopus 로고    scopus 로고
    • Nanoparticle-supported consecutive reactions catalyzed by alkyl hydroperoxide reductase
    • Wang L, Chen Y, Jiang R (2012) Nanoparticle-supported consecutive reactions catalyzed by alkyl hydroperoxide reductase. J Mol Catal B: Enzym 76: 9-14
    • (2012) J Mol Catal B: Enzym , vol.76 , pp. 9-14
    • Wang, L.1    Chen, Y.2    Jiang, R.3
  • 31
    • 79952444750 scopus 로고    scopus 로고
    • Activity and stability comparison of immobilized NADH oxidase on multi-walled carbon nanotubes, carbon nanospheres, and single-walled carbon nanotubes
    • Wang L, Xu R, Chen Y, Jiang R (2011a) Activity and stability comparison of immobilized NADH oxidase on multi-walled carbon nanotubes, carbon nanospheres, and single-walled carbon nanotubes. J Mol Catal B: Enzym 69(3-4): 120-126
    • (2011) J Mol Catal B: Enzym , vol.69 , Issue.3-4 , pp. 120-126
    • Wang, L.1    Xu, R.2    Chen, Y.3    Jiang, R.4
  • 32
    • 84863833347 scopus 로고    scopus 로고
    • Nanotubesupported Bioproduction of 4-hydroxy-2-butanone Via in Situ Cofactor Regeneration
    • doi: 10.1007/s00253-011-3699-z
    • Wang L, Zhang H, Ching C-B, Chen Y, Jiang RR (2011b) Nanotubesupported bioproduction of 4-hydroxy-2-butanone via in situ cofactor regeneration. Appl Microbiol Biotechnol. doi: 10.1007/s00253-011-3699-z
    • (2011) Appl Microbiol Biotechnol
    • Wang, L.1    Zhang, H.2    Ching, C.-B.3    Chen, Y.4    Jiang, R.R.5
  • 33
    • 33750002912 scopus 로고    scopus 로고
    • The group B Streptococcus NADH oxidase nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence
    • Yamamoto Y, Pargade V, Lamberet G, Gaudu P, Thomas F, Texereau J, Gruss A, Trieu-Cuot P, Poyart C (2006) The group B Streptococcus NADH oxidase nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence. Mol Microbiol 62(3): 772-785
    • (2006) Mol Microbiol , vol.62 , Issue.3 , pp. 772-785
    • Yamamoto, Y.1    Pargade, V.2    Lamberet, G.3    Gaudu, P.4    Thomas, F.5    Texereau, J.6    Gruss, A.7    Trieu-Cuot, P.8    Poyart, C.9


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