These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

136 related items for PubMed ID: 10224050

  • 1. Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase.
    Rothery RA, Trieber CA, Weiner JH.
    J Biol Chem; 1999 May 07; 274(19):13002-9. PubMed ID: 10224050
    [Abstract] [Full Text] [Related]

  • 2. Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion.
    Tang H, Rothery RA, Voss JE, Weiner JH.
    J Biol Chem; 2011 Apr 29; 286(17):15147-54. PubMed ID: 21357619
    [Abstract] [Full Text] [Related]

  • 3. Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase.
    Rothery RA, Weiner JH.
    Biochemistry; 1996 Mar 12; 35(10):3247-57. PubMed ID: 8605160
    [Abstract] [Full Text] [Related]

  • 4. Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase.
    Cheng VW, Rothery RA, Bertero MG, Strynadka NC, Weiner JH.
    Biochemistry; 2005 Jun 07; 44(22):8068-77. PubMed ID: 15924426
    [Abstract] [Full Text] [Related]

  • 5. Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster.
    Rothery RA, Weiner JH.
    Biochemistry; 1993 Jun 08; 32(22):5855-61. PubMed ID: 8389193
    [Abstract] [Full Text] [Related]

  • 6. Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase.
    Trieber CA, Rothery RA, Weiner JH.
    J Biol Chem; 1996 Nov 01; 271(44):27339-45. PubMed ID: 8910310
    [Abstract] [Full Text] [Related]

  • 7. Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli.
    Cammack R, Weiner JH.
    Biochemistry; 1990 Sep 11; 29(36):8410-6. PubMed ID: 2174699
    [Abstract] [Full Text] [Related]

  • 8. A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase.
    Tang H, Rothery RA, Weiner JH.
    Biochim Biophys Acta; 2013 Jun 11; 1827(6):730-7. PubMed ID: 23481370
    [Abstract] [Full Text] [Related]

  • 9. Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase.
    Trieber CA, Rothery RA, Weiner JH.
    J Biol Chem; 1996 Mar 01; 271(9):4620-6. PubMed ID: 8617723
    [Abstract] [Full Text] [Related]

  • 10. The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters.
    Rothery RA, Magalon A, Giordano G, Guigliarelli B, Blasco F, Weiner JH.
    J Biol Chem; 1998 Mar 27; 273(13):7462-9. PubMed ID: 9516445
    [Abstract] [Full Text] [Related]

  • 11. Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion.
    Jacques JG, Fourmond V, Arnoux P, Sabaty M, Etienne E, Grosse S, Biaso F, Bertrand P, Pignol D, Léger C, Guigliarelli B, Burlat B.
    Biochim Biophys Acta; 2014 Feb 27; 1837(2):277-86. PubMed ID: 24212053
    [Abstract] [Full Text] [Related]

  • 12. Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate.
    Magalon A, Rothery RA, Giordano G, Blasco F, Weiner JH.
    J Bacteriol; 1997 Aug 27; 179(16):5037-45. PubMed ID: 9260944
    [Abstract] [Full Text] [Related]

  • 13. Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis.
    Rothery RA, Weiner JH.
    Biochemistry; 1991 Aug 27; 30(34):8296-305. PubMed ID: 1653010
    [Abstract] [Full Text] [Related]

  • 14. Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis.
    Hänzelmann P, Hernández HL, Menzel C, García-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H.
    J Biol Chem; 2004 Aug 13; 279(33):34721-32. PubMed ID: 15180982
    [Abstract] [Full Text] [Related]

  • 15. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism.
    Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P.
    Eur J Biochem; 1992 Jul 01; 207(1):61-8. PubMed ID: 1321049
    [Abstract] [Full Text] [Related]

  • 16. Electron transfer from heme bL to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI).
    Rothery RA, Blasco F, Weiner JH.
    Biochemistry; 2001 May 01; 40(17):5260-8. PubMed ID: 11318649
    [Abstract] [Full Text] [Related]

  • 17. Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase.
    Kowal AT, Werth MT, Manodori A, Cecchini G, Schröder I, Gunsalus RP, Johnson MK.
    Biochemistry; 1995 Sep 26; 34(38):12284-93. PubMed ID: 7547971
    [Abstract] [Full Text] [Related]

  • 18. Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy.
    Dridge EJ, Watts CA, Jepson BJ, Line K, Santini JM, Richardson DJ, Butler CS.
    Biochem J; 2007 Nov 15; 408(1):19-28. PubMed ID: 17688424
    [Abstract] [Full Text] [Related]

  • 19. Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine oxidase family of molybdenum-containing enzymes.
    Boll M, Fuchs G, Meier C, Trautwein A, El Kasmi A, Ragsdale SW, Buchanan G, Lowe DJ.
    J Biol Chem; 2001 Dec 21; 276(51):47853-62. PubMed ID: 11602591
    [Abstract] [Full Text] [Related]

  • 20. Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes.
    Augier V, Guigliarelli B, Asso M, Bertrand P, Frixon C, Giordano G, Chippaux M, Blasco F.
    Biochemistry; 1993 Mar 02; 32(8):2013-23. PubMed ID: 8383531
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 7.