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Journal Abstract Search

306 related items for PubMed ID: 10320337

  • 1. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5.
    Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O.
    Biochemistry; 1999 May 11; 38(19):6111-8. PubMed ID: 10320337
    [Abstract] [Full Text] [Related]

  • 2. Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5.
    Toyama H, Chen ZW, Fukumoto M, Adachi O, Matsushita K, Mathews FS.
    J Mol Biol; 2005 Sep 09; 352(1):91-104. PubMed ID: 16061256
    [Abstract] [Full Text] [Related]

  • 3. Azurin involved in alcohol oxidation system in Pseudomonas putida HK5: expression analysis and gene cloning.
    Toyama H, Aoki N, Matsushita K, Adachi O.
    Biosci Biotechnol Biochem; 2001 Jul 09; 65(7):1617-26. PubMed ID: 11515547
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  • 4. The amino acid sequence of Pseudomonas putida azurin.
    Barber MJ, Trimboli AJ, McIntire WS.
    Arch Biochem Biophys; 1993 May 15; 303(1):22-6. PubMed ID: 8489263
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  • 5. Molecular cloning of quinohemoprotein alcohol dehydrogenase, ADH IIB, from Pseudomonas putida HK5.
    Toyama H, Fujii T, Aoki N, Matsushita K, Adachi O.
    Biosci Biotechnol Biochem; 2003 Jun 15; 67(6):1397-400. PubMed ID: 12843671
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  • 7. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.
    Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O.
    J Bacteriol; 1995 May 15; 177(9):2442-50. PubMed ID: 7730276
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  • 9. Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes in Pseudomonas putida HK5.
    Promden W, Vangnai AS, Pongsawasdi P, Adachi O, Matsushita K, Toyama H.
    FEMS Microbiol Lett; 2008 Mar 15; 280(2):203-9. PubMed ID: 18218017
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  • 11. The membrane-bound quinohemoprotein alcohol dehydrogenase from Gluconacetobacter diazotrophicus PAL5 carries a [2Fe-2S] cluster.
    Gómez-Manzo S, Solano-Peralta A, Saucedo-Vázquez JP, Escamilla-Marván JE, Kroneck PM, Sosa-Torres ME.
    Biochemistry; 2010 Mar 23; 49(11):2409-15. PubMed ID: 20148520
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  • 12. Identification and characterization of the AgmR regulator of Pseudomonas putida: role in alcohol utilization.
    Vrionis HA, Daugulis AJ, Kropinski AM.
    Appl Microbiol Biotechnol; 2002 Mar 23; 58(4):469-75. PubMed ID: 11954793
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  • 13. Mimicking protein-protein electron transfer: voltammetry of Pseudomonas aeruginosa azurin and the Thermus thermophilus Cu(A) domain at omega-derivatized self-assembled-monolayer gold electrodes.
    Fujita K, Nakamura N, Ohno H, Leigh BS, Niki K, Gray HB, Richards JH.
    J Am Chem Soc; 2004 Nov 03; 126(43):13954-61. PubMed ID: 15506756
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  • 14. Optical investigation of the electron transfer protein azurin-gold nanoparticle system.
    Delfino I, Cannistraro S.
    Biophys Chem; 2009 Jan 03; 139(1):1-7. PubMed ID: 18938024
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  • 16. Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity.
    Dewanti AR, Xu Y, Mitra B.
    Biochemistry; 2004 Aug 24; 43(33):10692-700. PubMed ID: 15311930
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  • 17. Axial methionine has much less influence on reduction potentials in a CuA center than in a blue copper center.
    Hwang HJ, Berry SM, Nilges MJ, Lu Y.
    J Am Chem Soc; 2005 May 25; 127(20):7274-5. PubMed ID: 15898751
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  • 18. Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures.
    Zhuravleva AV, Korzhnev DM, Kupce E, Arseniev AS, Billeter M, Orekhov VY.
    J Mol Biol; 2004 Oct 01; 342(5):1599-611. PubMed ID: 15364584
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  • 19. Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6.
    Kukimoto M, Nishiyama M, Tanokura M, Murphy ME, Adman ET, Horinouchi S.
    FEBS Lett; 1996 Sep 23; 394(1):87-90. PubMed ID: 8925934
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  • 20. Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X = Gly, Ala, Val, Leu, or Asp) mutants.
    Bonander N, Karlsson BG, Vänngård T.
    Biochemistry; 1996 Feb 20; 35(7):2429-36. PubMed ID: 8652586
    [Abstract] [Full Text] [Related]

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