메뉴 건너뛰기




Volumn 20, Issue 2, 2015, Pages 337-347

The biosynthesis of the molybdenum cofactors

Author keywords

bis MGD; cPMP; Molybdenum; Molybdenum cofactor; Sulfite oxidase; Sulfuration

Indexed keywords

COENZYME; CYCLIC PYRANOPTERIN PHOSPHATE; METALLOPROTEIN; MOLYBDENUM; MOLYBDENUM COFACTOR; NUCLEOTIDE; ORGANOPHOSPHORUS COMPOUND; OXIDOREDUCTASE; PTERIDINE DERIVATIVE; PTERIN DERIVATIVE;

EID: 84936750757     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-014-1173-y     Document Type: Article
Times cited : (96)

References (107)
  • 1
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • 1:CAS:528:DyaK38XksVeisr8%3D 1587808
    • Rajagopalan KV, Johnson JL (1992) The pterin molybdenum cofactors. J Biol Chem 267:10199-10202
    • (1992) J Biol Chem , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 2
    • 79952752769 scopus 로고    scopus 로고
    • The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria
    • 3081585 21528011
    • Leimkühler S, Wuebbens MM, Rajagopalan KV (2011) The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria. Coord Chem Rev 255:1129-1144
    • (2011) Coord Chem Rev , vol.255 , pp. 1129-1144
    • Leimkühler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 3
    • 84939913573 scopus 로고    scopus 로고
    • The biosynthesis of the molybdenum cofactor in Escherichia coli and its connection to FeS cluster assembly and the thiolation of tRNA
    • doi: 10.1155/2014/808569
    • Leimkühler S (2014) The biosynthesis of the molybdenum cofactor in Escherichia coli and its connection to FeS cluster assembly and the thiolation of tRNA. Adv Biol 2014. doi: 10.1155/2014/808569
    • (2014) Adv Biol 2014
    • Leimkühler, S.1
  • 4
    • 84877712159 scopus 로고    scopus 로고
    • The molybdenum cofactor
    • 3650355 1:CAS:528:DC%2BC3sXnsFSrurc%3D 23539623
    • Mendel RR (2013) The molybdenum cofactor. J Biol Chem 288:13165-13172
    • (2013) J Biol Chem , vol.288 , pp. 13165-13172
    • Mendel, R.R.1
  • 5
    • 79952744260 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis in plants and humans
    • 1:CAS:528:DC%2BC3MXjvVKqu7k%3D
    • Mendel RR, Schwarz G (2011) Molybdenum cofactor biosynthesis in plants and humans. Coord Chem Rev 255:1145-1158
    • (2011) Coord Chem Rev , vol.255 , pp. 1145-1158
    • Mendel, R.R.1    Schwarz, G.2
  • 6
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • 1:CAS:528:DyaK28Xmt1Gmsrg%3D 11848841
    • Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96:2757-2816
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 7
    • 84897972583 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • doi: 10.1021/cr400443z
    • Hille R, Hall J, Basu P (2014) The mononuclear molybdenum enzymes. Chem Rev 114(7):3963-4038. doi: 10.1021/cr400443z
    • (2014) Chem Rev , vol.114 , Issue.7 , pp. 3963-4038
    • Hille, R.1    Hall, J.2    Basu, P.3
  • 9
    • 0027444627 scopus 로고
    • Structural characterization of a molybdopterin precursor
    • 1:CAS:528:DyaK3sXlsFCltr0%3D 8514781
    • Wuebbens MM, Rajagopalan KV (1993) Structural characterization of a molybdopterin precursor. J Biol Chem 268:13493-13498
    • (1993) J Biol Chem , vol.268 , pp. 13493-13498
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 10
    • 0027490597 scopus 로고
    • In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene
    • 1:CAS:528:DyaK3sXmt1Shsb8%3D 8514783
    • Pitterle DM, Johnson JL, Rajagopalan KV (1993) In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene. J Biol Chem 268:13506-13509
    • (1993) J Biol Chem , vol.268 , pp. 13506-13509
    • Pitterle, D.M.1    Johnson, J.L.2    Rajagopalan, K.V.3
  • 11
    • 0029898124 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis in Escherichia coli mod and mog mutants
    • 178193 1:CAS:528:DyaK28Xktlyms70%3D 8763964
    • Joshi MS, Johnson JL, Rajagopalan KV (1996) Molybdenum cofactor biosynthesis in Escherichia coli mod and mog mutants. J Bacteriol 178:4310-4312
    • (1996) J Bacteriol , vol.178 , pp. 4310-4312
    • Joshi, M.S.1    Johnson, J.L.2    Rajagopalan, K.V.3
  • 12
    • 78651388592 scopus 로고    scopus 로고
    • Molybdopterin dinucleotide biosynthesis in Escherichia coli: Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides
    • 3020748 1:CAS:528:DC%2BC3MXjtFehtw%3D%3D 21081498
    • Neumann M, Seduk F, Iobbi-Nivol C, Leimkühler S (2011) Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides. J Biol Chem 286:1400-1408
    • (2011) J Biol Chem , vol.286 , pp. 1400-1408
    • Neumann, M.1    Seduk, F.2    Iobbi-Nivol, C.3    Leimkühler, S.4
  • 15
    • 84864303854 scopus 로고    scopus 로고
    • Cell biology of molybdenum in plants and humans
    • 1:CAS:528:DC%2BC38XjsFOnsLY%3D 22370186
    • Mendel RR, Kruse T (2012) Cell biology of molybdenum in plants and humans. Biochim Biophys Acta 1823:1568-1579
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1568-1579
    • Mendel, R.R.1    Kruse, T.2
  • 17
    • 0034058082 scopus 로고    scopus 로고
    • Genetics of molybdenum cofactor deficiency
    • 1:CAS:528:DC%2BD3cXivFaktrw%3D 10746556
    • Reiss J (2000) Genetics of molybdenum cofactor deficiency. Hum Genet 106:157-163
    • (2000) Hum Genet , vol.106 , pp. 157-163
    • Reiss, J.1
  • 18
    • 79952752115 scopus 로고    scopus 로고
    • Molybdenum enzymes in higher organisms
    • 3079273 1:CAS:528:DC%2BC3MXjvVKqu7c%3D 21516203
    • Hille R, Nishino T, Bittner F (2011) Molybdenum enzymes in higher organisms. Coord Chem Rev 255:1179-1205
    • (2011) Coord Chem Rev , vol.255 , pp. 1179-1205
    • Hille, R.1    Nishino, T.2    Bittner, F.3
  • 20
    • 0030317098 scopus 로고    scopus 로고
    • Molybdenum cofactor deficiency: Clinical presentation and laboratory diagnosis
    • Duran M, de Bree PK, de Klerk JBC, Dorland L, Berger R (1996) Molybdenum cofactor deficiency: clinical presentation and laboratory diagnosis. Int Pediatr 11:334-338
    • (1996) Int Pediatr , vol.11 , pp. 334-338
    • Duran, M.1    De Bree, P.K.2    De Klerk, J.B.C.3    Dorland, L.4    Berger, R.5
  • 21
    • 1942501738 scopus 로고    scopus 로고
    • The tetrahydropyranopterin structure of the sulfur- and metal-free molybdenum cofactor precursor
    • 1:CAS:528:DC%2BD2cXivF2qsrg%3D 14761975
    • Santamaria-Araujo JA, Fischer B, Otte T, Nimtz M, Mendel RR, Wray V, Schwarz G (2004) The tetrahydropyranopterin structure of the sulfur- and metal-free molybdenum cofactor precursor. J Biol Chem 279:15994-15999
    • (2004) J Biol Chem , vol.279 , pp. 15994-15999
    • Santamaria-Araujo, J.A.1    Fischer, B.2    Otte, T.3    Nimtz, M.4    Mendel, R.R.5    Wray, V.6    Schwarz, G.7
  • 22
    • 84877262019 scopus 로고    scopus 로고
    • Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis
    • 3777439 1:CAS:528:DC%2BC3sXmslSnu7k%3D 23627491
    • Hover BM, Loksztejn A, Ribeiro AA, Yokoyama K (2013) Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis. J Am Chem Soc 135:7019-7032
    • (2013) J Am Chem Soc , vol.135 , pp. 7019-7032
    • Hover, B.M.1    Loksztejn, A.2    Ribeiro, A.A.3    Yokoyama, K.4
  • 23
    • 84881067917 scopus 로고    scopus 로고
    • Molybdopterin biosynthesis: Trapping an unusual purine ribose adduct in the MoaA-catalyzed reaction
    • 3804160 1:CAS:528:DC%2BC3sXhtFSis7fK 23848839
    • Mehta AP, Abdelwahed SH, Begley TP (2013) Molybdopterin biosynthesis: trapping an unusual purine ribose adduct in the MoaA-catalyzed reaction. J Am Chem Soc 135:10883-10885
    • (2013) J Am Chem Soc , vol.135 , pp. 10883-10885
    • Mehta, A.P.1    Abdelwahed, S.H.2    Begley, T.P.3
  • 24
    • 0028819468 scopus 로고
    • Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies
    • 1:CAS:528:DyaK2MXjtFOksL4%3D 7836363
    • Wuebbens MM, Rajagopalan KV (1995) Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies. J Biol Chem 270:1082-1087
    • (1995) J Biol Chem , vol.270 , pp. 1082-1087
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 25
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • 29726 1:CAS:528:DC%2BD3MXhvFaqsLw%3D 11222759
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29:1097-1106
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 27
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • 516487 15317939
    • Hänzelmann P, Schindelin H (2004) Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc Natl Acad Sci USA 101:12870-12875
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12870-12875
    • Hänzelmann, P.1    Schindelin, H.2
  • 28
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
    • 1458979 16632608
    • Hänzelmann P, Schindelin H (2006) Binding of 5-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. Proc Natl Acad Sci USA 103:6829-6834
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6829-6834
    • Hänzelmann, P.1    Schindelin, H.2
  • 29
    • 0034661492 scopus 로고    scopus 로고
    • Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC
    • 1:CAS:528:DC%2BD3cXltVKjsb0%3D
    • Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H (2000) Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Struct Fold Des 8:709-718
    • (2000) Struct Fold des , vol.8 , pp. 709-718
    • Wuebbens, M.M.1    Liu, M.T.2    Rajagopalan, K.3    Schindelin, H.4
  • 31
    • 0032436716 scopus 로고    scopus 로고
    • Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A
    • 1:CAS:528:DyaK1cXnvFSjtb0%3D 9921896
    • Reiss J, Christensen E, Kurlemann G, Zabot M-T, Dorche C (1998) Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A. Hum Genet 103:639-644
    • (1998) Hum Genet , vol.103 , pp. 639-644
    • Reiss, J.1    Christensen, E.2    Kurlemann, G.3    Zabot, M.-T.4    Dorche, C.5
  • 32
    • 0036387191 scopus 로고    scopus 로고
    • The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons
    • Gross-Hard S, Reiss J (2002) The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons. Mol Genet Metab 76:340-343
    • (2002) Mol Genet Metab , vol.76 , pp. 340-343
    • Gross-Hard, S.1    Reiss, J.2
  • 33
    • 0033930936 scopus 로고    scopus 로고
    • Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames
    • 1369970 1:CAS:528:DC%2BD3cXlt1agtL0%3D 10917590
    • Gray TA, Nicholls RD (2000) Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames. RNA 6:928-936
    • (2000) RNA , vol.6 , pp. 928-936
    • Gray, T.A.1    Nicholls, R.D.2
  • 34
    • 0037166328 scopus 로고    scopus 로고
    • Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis
    • 11891227
    • Hänzelmann P, Schwarz G, Mendel RR (2002) Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis. J Biol Chem 277:18303-18312
    • (2002) J Biol Chem , vol.277 , pp. 18303-18312
    • Hänzelmann, P.1    Schwarz, G.2    Mendel, R.R.3
  • 36
    • 84939886887 scopus 로고
    • Molybdopterin formation by converting factor of E. Coli chlA1
    • Pitterle DM, Johnson JL, Rajagopalan KV (1990) Molybdopterin formation by converting factor of E. coli chlA1. FASEB J 4:A1957
    • (1990) FASEB J , vol.4 , pp. 1957
    • Pitterle, D.M.1    Johnson, J.L.2    Rajagopalan, K.V.3
  • 37
    • 0024352039 scopus 로고
    • Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1
    • 210060 1:CAS:528:DyaL1MXksFehtLw%3D 2656653
    • Pitterle DM, Rajagopalan KV (1989) Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1. J Bacteriol 171:3373-3378
    • (1989) J Bacteriol , vol.171 , pp. 3373-3378
    • Pitterle, D.M.1    Rajagopalan, K.V.2
  • 38
    • 84939884793 scopus 로고
    • Purification and characterization of the converting factor from E. Coli chlA1
    • Pitterle DM, Rajagopalan KV (1991) Purification and characterization of the converting factor from E. coli chlA1. FASEB J 5:A468
    • (1991) FASEB J , vol.5 , pp. 468
    • Pitterle, D.M.1    Rajagopalan, K.V.2
  • 39
    • 0027500718 scopus 로고
    • The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor
    • 1:CAS:528:DyaK3sXlslKnt78%3D 8514782
    • Pitterle DM, Rajagopalan KV (1993) The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. J Biol Chem 268:13499-13505
    • (1993) J Biol Chem , vol.268 , pp. 13499-13505
    • Pitterle, D.M.1    Rajagopalan, K.V.2
  • 40
    • 38849106821 scopus 로고    scopus 로고
    • Crystal structure of a molybdopterin synthase-precursor Z complex: Insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency
    • Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H (2008) Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency. Biochemistry 47(2):615-626
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 615-626
    • Daniels, J.N.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 41
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • 1:CAS:528:DC%2BD3MXjslyrsQ%3D%3D 11135669
    • Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H (2001) Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol 8:42-46
    • (2001) Nat Struct Biol , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 42
    • 0035965266 scopus 로고    scopus 로고
    • Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins
    • 1:CAS:528:DC%2BD3MXnt1yrsL0%3D 11459846
    • Gutzke G, Fischer B, Mendel RR, Schwarz G (2001) Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins. J Biol Chem 276:36268-36274
    • (2001) J Biol Chem , vol.276 , pp. 36268-36274
    • Gutzke, G.1    Fischer, B.2    Mendel, R.R.3    Schwarz, G.4
  • 43
    • 0038168025 scopus 로고    scopus 로고
    • Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency
    • 12732628
    • Leimkühler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR (2003) Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J Biol Chem 278:26127-26134
    • (2003) J Biol Chem , vol.278 , pp. 26127-26134
    • Leimkühler, S.1    Freuer, A.2    Araujo, J.A.3    Rajagopalan, K.V.4    Mendel, R.R.5
  • 44
    • 0038190972 scopus 로고    scopus 로고
    • Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis
    • 1:CAS:528:DC%2BD3sXjtVShtrs%3D 12571226
    • Wuebbens MM, Rajagopalan KV (2003) Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. J Biol Chem 278:14523-14532
    • (2003) J Biol Chem , vol.278 , pp. 14523-14532
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 45
    • 0035860726 scopus 로고    scopus 로고
    • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
    • 11463785
    • Leimkühler S, Wuebbens MM, Rajagopalan KV (2001) Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J Biol Chem 276:34695-34701
    • (2001) J Biol Chem , vol.276 , pp. 34695-34701
    • Leimkühler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 46
    • 45749149275 scopus 로고    scopus 로고
    • Evolutionary origin of the activation step during ubiquitin-dependent protein degradation
    • R.J. Mayer A. Ciechanover M. Rechsteiner (eds) WILEY-VCH Weinheim
    • Schindelin H (2005) Evolutionary origin of the activation step during ubiquitin-dependent protein degradation. In: Mayer RJ, Ciechanover A, Rechsteiner M (eds) Protein degradation: ubiquitin and the chemistry of life. WILEY-VCH, Weinheim, pp 21-43
    • (2005) Protein Degradation: Ubiquitin and the Chemistry of Life , pp. 21-43
    • Schindelin, H.1
  • 47
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • 1:CAS:528:DC%2BD3MXovFGisLg%3D 11713534
    • Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H (2001) Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414:325-329
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 48
    • 33846392698 scopus 로고    scopus 로고
    • Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold
    • 1:CAS:528:DC%2BD28Xhtlelt7jN 17223713
    • Schmitz J, Wuebbens MM, Rajagopalan KV, Leimkühler S (2007) Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry 46:909-916
    • (2007) Biochemistry , vol.46 , pp. 909-916
    • Schmitz, J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Leimkühler, S.4
  • 49
    • 14044252222 scopus 로고    scopus 로고
    • Thermodynamic analysis of subunit interactions in Escherichia coli molybdopterin synthase
    • 1:CAS:528:DC%2BD2MXhsFChsL0%3D 15709772
    • Tong Y, Wuebbens MM, Rajagopalan KV, Fitzgerald MC (2005) Thermodynamic analysis of subunit interactions in Escherichia coli molybdopterin synthase. Biochemistry 44:2595-2601
    • (2005) Biochemistry , vol.44 , pp. 2595-2601
    • Tong, Y.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Fitzgerald, M.C.4
  • 50
    • 0035933851 scopus 로고    scopus 로고
    • An Escherichia coli NifS-like sulfurtransferase is required for the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z
    • 11290749
    • Leimkühler S, Rajagopalan KV (2001) An Escherichia coli NifS-like sulfurtransferase is required for the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z. J Biol Chem 276:22024-22031
    • (2001) J Biol Chem , vol.276 , pp. 22024-22031
    • Leimkühler, S.1    Rajagopalan, K.V.2
  • 51
    • 77449106447 scopus 로고    scopus 로고
    • IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
    • 2807287 1:CAS:528:DC%2BC3cXlvFCnsw%3D%3D 19946146
    • Zhang W, Urban A, Mihara H, Leimkühler S, Kurihara T, Esaki N (2010) IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. J Biol Chem 285:2302-2308
    • (2010) J Biol Chem , vol.285 , pp. 2302-2308
    • Zhang, W.1    Urban, A.2    Mihara, H.3    Leimkühler, S.4    Kurihara, T.5    Esaki, N.6
  • 53
    • 80053905923 scopus 로고    scopus 로고
    • The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli
    • 3195606 1:CAS:528:DC%2BC3MXht1yhtrnJ 21856748
    • Dahl JU, Urban A, Bolte A, Sriyabhaya P, Donahue JL, Nimtz M, Larson TJ, Leimkühler S (2011) The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J Biol Chem 286:35801-35812
    • (2011) J Biol Chem , vol.286 , pp. 35801-35812
    • Dahl, J.U.1    Urban, A.2    Bolte, A.3    Sriyabhaya, P.4    Donahue, J.L.5    Nimtz, M.6    Larson, T.J.7    Leimkühler, S.8
  • 54
    • 84884343748 scopus 로고    scopus 로고
    • Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli
    • 1:CAS:528:DC%2BC38XhvVOjs73F 23201473
    • Iobbi-Nivol C, Leimkühler S (2013) Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli. Biochim Biophys Acta 1827:1086-1101
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 1086-1101
    • Iobbi-Nivol, C.1    Leimkühler, S.2
  • 55
    • 0033364822 scopus 로고    scopus 로고
    • Human molybdopterin synthase gene: Identification of a bicistronic transcript with overlapping reading frames
    • 1377786 1:CAS:528:DyaK1MXitFChtrc%3D 10053003
    • Stallmeyer B, Drugeon G, Reiss J, Haenni AL, Mendel RR (1999) Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames. Am J Hum Genet 64:698-705
    • (1999) Am J Hum Genet , vol.64 , pp. 698-705
    • Stallmeyer, B.1    Drugeon, G.2    Reiss, J.3    Haenni, A.L.4    Mendel, R.R.5
  • 56
    • 33748960018 scopus 로고    scopus 로고
    • A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase
    • Hahnewald R, Leimkühler S, Vilaseca A, Acquaviva-Bourdain C, Lenz U, Reiss J (2006) A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase. Mol Genet Metab 89(3):210-213
    • (2006) Mol Genet Metab , vol.89 , Issue.3 , pp. 210-213
    • Hahnewald R, L.1
  • 57
    • 1942533536 scopus 로고    scopus 로고
    • Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans
    • 395903 1:CAS:528:DC%2BD2cXjsFKnsL4%3D 15073332
    • Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (2004) Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc Natl Acad Sci USA 101:5946-5951
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5946-5951
    • Matthies, A.1    Rajagopalan, K.V.2    Mendel, R.R.3    Leimkühler, S.4
  • 58
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily
    • 1084204 1:CAS:528:DC%2BD38Xms1agtLo%3D 12151332
    • Bordo D, Bork P (2002) The rhodanese/Cdc25 phosphatase superfamily. EMBO Rep 3:741-746
    • (2002) EMBO Rep , vol.3 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 59
    • 19644366036 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis in humans: Identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry
    • 1:CAS:528:DC%2BD2MXjvVeiu7g%3D 15910006
    • Matthies A, Nimtz M, Leimkühler S (2005) Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44:7912-7920
    • (2005) Biochemistry , vol.44 , pp. 7912-7920
    • Matthies, A.1    Nimtz, M.2    Leimkühler, S.3
  • 60
    • 34249278086 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active-site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3: Major differences in substrate specificity between eukaryotic and bacterial homologues
    • 1:CAS:528:DC%2BD2sXmvVWrtb4%3D 17459099
    • Krepinsky K, Leimkühler S (2007) Site-directed mutagenesis of the active-site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3: major differences in substrate specificity between eukaryotic and bacterial homologues. FEBS J 274:2778-2787
    • (2007) FEBS J , vol.274 , pp. 2778-2787
    • Krepinsky, K.1    Leimkühler, S.2
  • 61
    • 54449085541 scopus 로고    scopus 로고
    • A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
    • 1:CAS:528:DC%2BD1cXhtVyisL3P 18650437
    • Marelja Z, Stöcklein W, Nimtz M, Leimkühler S (2008) A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J Biol Chem 283:25178-25185
    • (2008) J Biol Chem , vol.283 , pp. 25178-25185
    • Marelja, Z.1    Stöcklein, W.2    Nimtz, M.3    Leimkühler, S.4
  • 62
    • 0034695475 scopus 로고    scopus 로고
    • Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli
    • 1:CAS:528:DC%2BD3cXotFWrtQ%3D%3D 10636880
    • Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H (2000) Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli. J Biol Chem 275:1814-1822
    • (2000) J Biol Chem , vol.275 , pp. 1814-1822
    • Liu, M.T.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 63
    • 0034880831 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin
    • 1:CAS:528:DC%2BD3MXjsValsr0%3D 11525167
    • Xiang S, Nichols J, Rajagopalan KV, Schindelin H (2001) The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure 9:299-310
    • (2001) Structure , vol.9 , pp. 299-310
    • Xiang, S.1    Nichols, J.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 64
    • 0035816219 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway
    • 1:CAS:528:DC%2BD3MXks1OrsLs%3D 11428898
    • Schrag JD, Huang W, Sivaraman J, Smith C, Plamondon J, Larocque R, Matte A, Cygler M (2001) The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J Mol Biol 310:419-431
    • (2001) J Mol Biol , vol.310 , pp. 419-431
    • Schrag, J.D.1    Huang, W.2    Sivaraman, J.3    Smith, C.4    Plamondon, J.5    Larocque, R.6    Matte, A.7    Cygler, M.8
  • 65
    • 0037067684 scopus 로고    scopus 로고
    • Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis
    • 1:CAS:528:DC%2BD38XlsVWitL8%3D 12006571
    • Nichols J, Rajagopalan KV (2002) Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis. J Biol Chem 277:24995-25000
    • (2002) J Biol Chem , vol.277 , pp. 24995-25000
    • Nichols, J.1    Rajagopalan, K.V.2
  • 66
    • 14844331741 scopus 로고    scopus 로고
    • In vitro molybdenum ligation to molybdopterin using purified components
    • 1:CAS:528:DC%2BD2MXhs1yitro%3D 15632135
    • Nichols JD, Rajagopalan KV (2005) In vitro molybdenum ligation to molybdopterin using purified components. J Biol Chem 280:7817-7822
    • (2005) J Biol Chem , vol.280 , pp. 7817-7822
    • Nichols, J.D.1    Rajagopalan, K.V.2
  • 67
    • 0029394803 scopus 로고
    • Molybdenum cofactor biosynthesis: The A thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three E. Coli proteins
    • 1:CAS:528:DyaK28Xis1KgsA%3D%3D 8528286
    • Stallmeyer B, Nerlich A, Schiemann J, Brinkmann H, Mendel RR (1995) Molybdenum cofactor biosynthesis: the A. thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three E. coli proteins. Plant J 8:751-762
    • (1995) Plant J , vol.8 , pp. 751-762
    • Stallmeyer, B.1    Nerlich, A.2    Schiemann, J.3    Brinkmann, H.4    Mendel, R.R.5
  • 68
    • 0033574072 scopus 로고    scopus 로고
    • The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells
    • 15463 1:CAS:528:DyaK1MXhsFSrtb4%3D 9990024
    • Stallmeyer B, Schwarz G, Schulze J, Nerlich A, Reiss J, Kirsch J, Mendel RR (1999) The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells. Proc Natl Acad Sci USA 96:1333-1338
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1333-1338
    • Stallmeyer, B.1    Schwarz, G.2    Schulze, J.3    Nerlich, A.4    Reiss, J.5    Kirsch, J.6    Mendel, R.R.7
  • 69
    • 4043114792 scopus 로고    scopus 로고
    • Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism
    • 1:CAS:528:DC%2BD2cXmsVGlsr0%3D 15306815
    • Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G (2004) Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism. Nature 430:803-806
    • (2004) Nature , vol.430 , pp. 803-806
    • Kuper, J.1    Llamas, A.2    Hecht, H.J.3    Mendel, R.R.4    Schwarz, G.5
  • 70
    • 11244333112 scopus 로고    scopus 로고
    • Synthesis of adenylated molybdopterin: An essential step for molybdenum insertion
    • 1:CAS:528:DC%2BD2cXhtFeis7zE 15504727
    • Llamas A, Mendel RR, Schwarz G (2004) Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion. J Biol Chem 279:55241-55246
    • (2004) J Biol Chem , vol.279 , pp. 55241-55246
    • Llamas, A.1    Mendel, R.R.2    Schwarz, G.3
  • 71
    • 33745863101 scopus 로고    scopus 로고
    • The mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly
    • 1:CAS:528:DC%2BD28XmsVagsb0%3D 16636046
    • Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G (2006) The mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly. J Biol Chem 281:18343-18350
    • (2006) J Biol Chem , vol.281 , pp. 18343-18350
    • Llamas, A.1    Otte, T.2    Multhaup, G.3    Mendel, R.R.4    Schwarz, G.5
  • 72
    • 84873031594 scopus 로고    scopus 로고
    • Metal insertion into the molybdenum cofactor: Product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin
    • 1:CAS:528:DC%2BC3sXht1CgsLk%3D 23163752
    • Belaidi AA, Schwarz G (2013) Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. Biochem J 450:149-157
    • (2013) Biochem J , vol.450 , pp. 149-157
    • Belaidi, A.A.1    Schwarz, G.2
  • 73
    • 35348909569 scopus 로고    scopus 로고
    • Probing the role of copper in the biosynthesis of the molybdenum cofactor in Escherichia coli and Rhodobacter sphaeroides
    • 1:CAS:528:DC%2BD2sXhtFKrsb3M 17687573
    • Morrison MS, Cobine PA, Hegg EL (2007) Probing the role of copper in the biosynthesis of the molybdenum cofactor in Escherichia coli and Rhodobacter sphaeroides. J Biol Inorg Chem 12:1129-1139
    • (2007) J Biol Inorg Chem , vol.12 , pp. 1129-1139
    • Morrison, M.S.1    Cobine, P.A.2    Hegg, E.L.3
  • 74
    • 0035910397 scopus 로고    scopus 로고
    • In vitro incorporation of nascent molybdenum cofactor into human sulfite oxidase
    • 11042213
    • Leimkühler S, Rajagopalan KV (2001) In vitro incorporation of nascent molybdenum cofactor into human sulfite oxidase. J Biol Chem 276:1837-1844
    • (2001) J Biol Chem , vol.276 , pp. 1837-1844
    • Leimkühler, S.1    Rajagopalan, K.V.2
  • 75
    • 28844475146 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and deficiency
    • 1:CAS:528:DC%2BD28XhsVWqtA%3D%3D 16261263
    • Schwarz G (2005) Molybdenum cofactor biosynthesis and deficiency. Cell Mol Life Sci 62:2792-2810
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2792-2810
    • Schwarz, G.1
  • 76
    • 84859760208 scopus 로고    scopus 로고
    • Splice-specific glycine receptor binding, folding, and phosphorylation of the scaffolding protein gephyrin
    • 3339950 1:CAS:528:DC%2BC38XlsFCju7g%3D 22351777
    • Herweg J, Schwarz G (2012) Splice-specific glycine receptor binding, folding, and phosphorylation of the scaffolding protein gephyrin. J Biol Chem 287:12645-12656
    • (2012) J Biol Chem , vol.287 , pp. 12645-12656
    • Herweg, J.1    Schwarz, G.2
  • 77
    • 0034704126 scopus 로고    scopus 로고
    • Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • 1:CAS:528:DC%2BD3MXhsFemtw%3D%3D 10978348
    • Temple CA, Rajagopalan KV (2000) Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J Biol Chem 275:40202-40210
    • (2000) J Biol Chem , vol.275 , pp. 40202-40210
    • Temple, C.A.1    Rajagopalan, K.V.2
  • 78
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mob gene products in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • 1:CAS:528:DyaK28XjsFGjt7w%3D 8793883
    • Palmer T, Santini C-L, Iobbi-Nivol C, Eaves DJ, Boxer DH, Giordano G (1996) Involvement of the narJ and mob gene products in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol Microbiol 20:875-884
    • (1996) Mol Microbiol , vol.20 , pp. 875-884
    • Palmer, T.1    Santini, C.-L.2    Iobbi-Nivol, C.3    Eaves, D.J.4    Boxer, D.H.5    Giordano, G.6
  • 79
    • 0034704163 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis
    • 1:CAS:528:DC%2BD3MXhsFemtA%3D%3D 10978347
    • Lake MW, Temple CA, Rajagopalan KV, Schindelin H (2000) The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. J Biol Chem 275:40211-40217
    • (2000) J Biol Chem , vol.275 , pp. 40211-40217
    • Lake, M.W.1    Temple, C.A.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 80
    • 0034435586 scopus 로고    scopus 로고
    • Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution
    • 1:CAS:528:DC%2BD3cXotVOiu7g%3D
    • Stevenson CE, Sargent F, Buchanan G, Palmer T, Lawson DM (2000) Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Struct Fold Des 8:1115-1125
    • (2000) Struct Fold des , vol.8 , pp. 1115-1125
    • Stevenson, C.E.1    Sargent, F.2    Buchanan, G.3    Palmer, T.4    Lawson, D.M.5
  • 81
    • 84856907383 scopus 로고    scopus 로고
    • A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli
    • 3281601 1:CAS:528:DC%2BC38XitFagsrk%3D 22194618
    • Thome R, Gust A, Toci R, Mendel R, Bittner F, Magalon A, Walburger A (2012) A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli. J Biol Chem 287:4671-4678
    • (2012) J Biol Chem , vol.287 , pp. 4671-4678
    • Thome, R.1    Gust, A.2    Toci, R.3    Mendel, R.4    Bittner, F.5    Magalon, A.6    Walburger, A.7
  • 82
    • 33748337941 scopus 로고    scopus 로고
    • Formate-reduced E. Coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism
    • 1:CAS:528:DC%2BD28XptVWrtr0%3D 16830149
    • Raaijmakers HC, Romao MJ (2006) Formate-reduced E. coli formate dehydrogenase H: the reinterpretation of the crystal structure suggests a new reaction mechanism. J Biol Inorg Chem 11:849-854
    • (2006) J Biol Inorg Chem , vol.11 , pp. 849-854
    • Raaijmakers, H.C.1    Romao, M.J.2
  • 83
    • 79955478107 scopus 로고    scopus 로고
    • The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states
    • 1:CAS:528:DC%2BC3MXltFegsrY%3D 21419779
    • Coelho C, Gonzalez PJ, Moura JG, Moura I, Trincao J, Joao Romao M (2011) The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states. J Mol Biol 408:932-948
    • (2011) J Mol Biol , vol.408 , pp. 932-948
    • Coelho, C.1    Gonzalez, P.J.2    Moura, J.G.3    Moura, I.4    Trincao, J.5    Joao Romao, M.6
  • 84
    • 69249111693 scopus 로고    scopus 로고
    • MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli
    • 2755913 1:CAS:528:DC%2BD1MXpsFymtro%3D 19542235
    • Neumann M, Mittelstädt G, Seduk F, Iobbi-Nivol C, Leimkühler S (2009) MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli. J Biol Chem 284:21891-21898
    • (2009) J Biol Chem , vol.284 , pp. 21891-21898
    • Neumann, M.1    Mittelstädt, G.2    Seduk, F.3    Iobbi-Nivol, C.4    Leimkühler, S.5
  • 85
    • 79251591929 scopus 로고    scopus 로고
    • The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria
    • 2997495 21151514
    • Neumann M, Leimkühler S (2011) The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria. Biochem Res Int 2011:850924
    • (2011) Biochem Res Int , vol.2011 , pp. 850924
    • Neumann, M.1    Leimkühler, S.2
  • 86
    • 34548080081 scopus 로고    scopus 로고
    • Identification of a Rhodobacter capsulatus l-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase
    • 1:CAS:528:DC%2BD2sXotVKht74%3D 17649978
    • Neumann M, Stöcklein W, Walburger A, Magalon A, Leimkühler S (2007) Identification of a Rhodobacter capsulatus l-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase. Biochemistry 46:9586-9595
    • (2007) Biochemistry , vol.46 , pp. 9586-9595
    • Neumann, M.1    Stöcklein, W.2    Walburger, A.3    Magalon, A.4    Leimkühler, S.5
  • 87
    • 35348938460 scopus 로고    scopus 로고
    • Transfer of the molybdenum cofactor synthesized by Rhodobacter capsulatus MoeA to XdhC and MobA
    • 1:CAS:528:DC%2BD2sXhtVOmtb%2FE 17686778
    • Neumann M, Stöcklein W, Leimkühler S (2007) Transfer of the molybdenum cofactor synthesized by Rhodobacter capsulatus MoeA to XdhC and MobA. J Biol Chem 282:28493-28500
    • (2007) J Biol Chem , vol.282 , pp. 28493-28500
    • Neumann, M.1    Stöcklein, W.2    Leimkühler, S.3
  • 88
    • 0035798636 scopus 로고    scopus 로고
    • ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana
    • 1:CAS:528:DC%2BD3MXosVKhsbc%3D 11553608
    • Bittner F, Oreb M, Mendel RR (2001) ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J Biol Chem 276:40381-40384
    • (2001) J Biol Chem , vol.276 , pp. 40381-40384
    • Bittner, F.1    Oreb, M.2    Mendel, R.R.3
  • 89
    • 14244265322 scopus 로고    scopus 로고
    • Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration
    • 1:CAS:528:DC%2BD2MXhtVynurs%3D 15561708
    • Heidenreich T, Wollers S, Mendel RR, Bittner F (2005) Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J Biol Chem 280:4213-4218
    • (2005) J Biol Chem , vol.280 , pp. 4213-4218
    • Heidenreich, T.1    Wollers, S.2    Mendel, R.R.3    Bittner, F.4
  • 90
    • 44349189896 scopus 로고    scopus 로고
    • Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration
    • 1:CAS:528:DC%2BD1cXkt1aksL8%3D 18258600
    • Wollers S, Heidenreich T, Zarepour M, Zachmann D, Kraft C, Zhao Y, Mendel RR, Bittner F (2008) Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J Biol Chem 283:9642-9650
    • (2008) J Biol Chem , vol.283 , pp. 9642-9650
    • Wollers, S.1    Heidenreich, T.2    Zarepour, M.3    Zachmann, D.4    Kraft, C.5    Zhao, Y.6    Mendel, R.R.7    Bittner, F.8
  • 91
    • 84855923018 scopus 로고    scopus 로고
    • Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis
    • 1:CAS:528:DC%2BC38XovFKkug%3D%3D 22004669
    • Lehrke M, Rump S, Heidenreich T, Wissing J, Mendel RR, Bittner F (2012) Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis. Biochem J 441:823-832
    • (2012) Biochem J , vol.441 , pp. 823-832
    • Lehrke, M.1    Rump, S.2    Heidenreich, T.3    Wissing, J.4    Mendel, R.R.5    Bittner, F.6
  • 92
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • 1:CAS:528:DyaK2sXktFOiu74%3D 9242907
    • Kisker C, Schindelin H, Rees DC (1997) Molybdenum-cofactor-containing enzymes: structure and mechanism. Ann Rev Biochem 66:233-267
    • (1997) Ann Rev Biochem , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 93
    • 67650760575 scopus 로고    scopus 로고
    • Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes
    • 1:CAS:528:DC%2BD1MXosl2kurk%3D 19519768
    • Genest O, Mejean V, Iobbi-Nivol C (2009) Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes. FEMS Microbiol Lett 297:1-9
    • (2009) FEMS Microbiol Lett , vol.297 , pp. 1-9
    • Genest, O.1    Mejean, V.2    Iobbi-Nivol, C.3
  • 94
    • 84896725626 scopus 로고    scopus 로고
    • The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor
    • 24444607
    • Böhmer N, Hartmann T, Leimkühler S (2014) The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor. FEBS Lett 588:531-537
    • (2014) FEBS Lett , vol.588 , pp. 531-537
    • Böhmer, N.1    Hartmann, T.2    Leimkühler, S.3
  • 95
    • 0032540896 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopterin cofactor in a molybdate charged form
    • 1:CAS:528:DyaK1cXks1KqtrY%3D 9708903
    • Witte CP, Igeno MI, Mendel R, Schwarz G, Fernandez E (1998) The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopterin cofactor in a molybdate charged form. FEBS Lett 431:205-209
    • (1998) FEBS Lett , vol.431 , pp. 205-209
    • Witte, C.P.1    Igeno, M.I.2    Mendel, R.3    Schwarz, G.4    Fernandez, E.5
  • 97
    • 77949891886 scopus 로고    scopus 로고
    • Identification and biochemical characterization of molybdenum cofactor-binding proteins from Arabidopsis thaliana
    • 2825458 1:CAS:528:DC%2BC3cXit1aisbc%3D 20040598
    • Kruse T, Gehl C, Geisler M, Lehrke M, Ringel P, Hallier S, Hansch R, Mendel RR (2010) Identification and biochemical characterization of molybdenum cofactor-binding proteins from Arabidopsis thaliana. J Biol Chem 285:6623-6635
    • (2010) J Biol Chem , vol.285 , pp. 6623-6635
    • Kruse, T.1    Gehl, C.2    Geisler, M.3    Lehrke, M.4    Ringel, P.5    Hallier, S.6    Hansch, R.7    Mendel, R.R.8
  • 98
    • 8144225875 scopus 로고    scopus 로고
    • Coordinating assembly and export of complex bacterial proteins
    • 524343 1:CAS:528:DC%2BD2cXotlCrs7o%3D 15385959
    • Jack RL, Buchanan G, Dubini A, Hatzixanthis K, Palmer T, Sargent F (2004) Coordinating assembly and export of complex bacterial proteins. EMBO J 23:3962-3972
    • (2004) EMBO J , vol.23 , pp. 3962-3972
    • Jack, R.L.1    Buchanan, G.2    Dubini, A.3    Hatzixanthis, K.4    Palmer, T.5    Sargent, F.6
  • 99
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • 1:CAS:528:DyaK28XmvVygt7Y%3D 8939424
    • Berks BC (1996) A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22:393-404
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 100
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • 1:CAS:528:DC%2BD2MXivFSlsbY%3D 15802249
    • Berks BC, Palmer T, Sargent F (2005) Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr Opin Microbiol 8:174-181
    • (2005) Curr Opin Microbiol , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 101
    • 3042660859 scopus 로고    scopus 로고
    • Physiological roles of xanthine oxidoreductase
    • 1:CAS:528:DC%2BD2cXksVSmu7s%3D 15237859
    • Harrison R (2004) Physiological roles of xanthine oxidoreductase. Drug Metab Rev 36:363-375
    • (2004) Drug Metab Rev , vol.36 , pp. 363-375
    • Harrison, R.1
  • 102
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • 1223366 1:CAS:528:DC%2BD3sXjsFeitbg%3D 12578558
    • Garattini E, Mendel R, Romao MJ, Wright R, Terao M (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372:15-32
    • (2003) Biochem J , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 104
    • 84871140998 scopus 로고    scopus 로고
    • Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways
    • 1:CAS:528:DC%2BC3sXhs1OhtbY%3D 22854042
    • Klein JM, Schwarz G (2012) Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. J Cell Sci 125:4876-4885
    • (2012) J Cell Sci , vol.125 , pp. 4876-4885
    • Klein, J.M.1    Schwarz, G.2
  • 105
    • 84880051185 scopus 로고    scopus 로고
    • The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells
    • 3711290 1:CAS:528:DC%2BC3sXhtV2ru73E 23703616
    • Plitzko B, Ott G, Reichmann D, Henderson CJ, Wolf CR, Mendel R, Bittner F, Clement B, Havemeyer A (2013) The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. J Biol Chem 288:20228-20237
    • (2013) J Biol Chem , vol.288 , pp. 20228-20237
    • Plitzko, B.1    Ott, G.2    Reichmann, D.3    Henderson, C.J.4    Wolf, C.R.5    Mendel, R.6    Bittner, F.7    Clement, B.8    Havemeyer, A.9
  • 106
    • 84871168534 scopus 로고    scopus 로고
    • The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-anchored protein of the outer mitochondrial membrane
    • 3525010 1:CAS:528:DC%2BC38XhvVeksbrJ 23086957
    • Klein JM, Busch JD, Potting C, Baker MJ, Langer T, Schwarz G (2012) The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-anchored protein of the outer mitochondrial membrane. J Biol Chem 287:42795-42803
    • (2012) J Biol Chem , vol.287 , pp. 42795-42803
    • Klein, J.M.1    Busch, J.D.2    Potting, C.3    Baker, M.J.4    Langer, T.5    Schwarz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.