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Volumn 8, Issue 2, 2013, Pages

Bacillus megaterium Has Both a Functional BluB Protein Required for DMB Synthesis and a Related Flavoprotein That Forms a Stable Radical Species

Author keywords

[No Author keywords available]

Indexed keywords

4A PEROXYFLAVIN; BACTERIAL PROTEIN; COBINAMIDE; CYANOCOBALAMIN; FLAVOPROTEIN; OXYGEN; PROTEIN BLUB; SCAVENGER; SEMIQUINONE; UNCLASSIFIED DRUG; VITAMIN B GROUP;

EID: 84874006797     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055708     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 33947529225 scopus 로고    scopus 로고
    • BluB cannibalizes flavin to form the lower ligand of vitamin B12
    • Taga M, Larsen N, Howard-Jones A, Walsh C, Walker G, (2007) BluB cannibalizes flavin to form the lower ligand of vitamin B12. Nature 446: 449-453.
    • (2007) Nature , vol.446 , pp. 449-453
    • Taga, M.1    Larsen, N.2    Howard-Jones, A.3    Walsh, C.4    Walker, G.5
  • 4
    • 0002449548 scopus 로고    scopus 로고
    • Chapter 22: Biosynthesis of the 5,6-dimethylbenzimidazole moiety of cobalamin and of the other bases found in natural corrinoids
    • Renz P, (1999) Chapter 22: Biosynthesis of the 5,6-dimethylbenzimidazole moiety of cobalamin and of the other bases found in natural corrinoids. In: Chemistry and Biochemistry of Banerjee R, editor. B12: 557-575.
    • (1999) Chemistry and Biochemistry of , vol.B12 , pp. 557-575
    • Renz, P.1    Banerjee, R.2
  • 6
    • 0000514262 scopus 로고
    • Biosynthesis of 5, 6-dimethylbenzimidazole from riboflavin Transformation of C-1′ of riboflavin into C-2 of 5, 6-dimethylbenzimidazole
    • Renz P, Weyhenmeyer R, (1972) Biosynthesis of 5, 6-dimethylbenzimidazole from riboflavin Transformation of C-1′ of riboflavin into C-2 of 5, 6-dimethylbenzimidazole. FEBS Letters 22: 124.
    • (1972) FEBS Letters , vol.22 , pp. 124
    • Renz, P.1    Weyhenmeyer, R.2
  • 7
    • 0141853263 scopus 로고    scopus 로고
    • Formation of the dimethylbenzimidazole ligand of coenzyme B12 under physiological conditions by a facile oxidative cascade
    • Maggio-Hall L, Dorrestein P, Escalante-Semerena J, Begley T, (2003) Formation of the dimethylbenzimidazole ligand of coenzyme B12 under physiological conditions by a facile oxidative cascade. Organic Letters 5: 2211-2213.
    • (2003) Organic Letters , vol.5 , pp. 2211-2213
    • Maggio-Hall, L.1    Dorrestein, P.2    Escalante-Semerena, J.3    Begley, T.4
  • 11
    • 0032189235 scopus 로고    scopus 로고
    • Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon
    • Raux E, Lanois A, Warren M, Rambach A, Thermes C, (1998) Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Biochemical Journal 335: 159.
    • (1998) Biochemical Journal , vol.335 , pp. 159
    • Raux, E.1    Lanois, A.2    Warren, M.3    Rambach, A.4    Thermes, C.5
  • 13
    • 0029090774 scopus 로고
    • Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus
    • Pollich M, Klug G, (1995) Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. Journal of Bacteriology 177: 4481.
    • (1995) Journal of Bacteriology , vol.177 , pp. 4481
    • Pollich, M.1    Klug, G.2
  • 15
    • 38949170703 scopus 로고    scopus 로고
    • One Pathway Can Incorporate either Adenine or Dimethylbenzimidazole as an {alpha}-Axial Ligand of B12 Cofactors in Salmonella enterica
    • Anderson PJ, Lango J, Carkeet C, Britten A, Krautler B, et al. (2008) One Pathway Can Incorporate either Adenine or Dimethylbenzimidazole as an {alpha}-Axial Ligand of B12 Cofactors in Salmonella enterica. Journal of Bacteriology 190: 1160.
    • (2008) Journal of Bacteriology , vol.190 , pp. 1160
    • Anderson, P.J.1    Lango, J.2    Carkeet, C.3    Britten, A.4    Krautler, B.5
  • 16
    • 0026657140 scopus 로고
    • Autogenous regulation of ethanolamine utilization by a transcriptional activator of the eut operon in Salmonella typhimurium
    • Roof DM, Roth JR, (1992) Autogenous regulation of ethanolamine utilization by a transcriptional activator of the eut operon in Salmonella typhimurium. J Bacteriol 174: 6634-6643.
    • (1992) J Bacteriol , vol.174 , pp. 6634-6643
    • Roof, D.M.1    Roth, J.R.2
  • 17
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J, (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. Journal of Bacteriology 177: 4121-4130.
    • (1995) Journal of Bacteriology , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 18
    • 0028063385 scopus 로고
    • The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin
    • O'Toole GA, Trzebiatowski JR, Escalante-Semerena JC, (1994) The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. Journal of Biological Chemistry 269: 26503-26511.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 26503-26511
    • O'Toole, G.A.1    Trzebiatowski, J.R.2    Escalante-Semerena, J.C.3
  • 19
    • 0025608395 scopus 로고
    • Isolation and characterization of levansucrase-encoding gene from Bacillus amyloliquefaciens
    • Tang LB, Lenstra R, Borchert TV, Nagarajan V, (1990) Isolation and characterization of levansucrase-encoding gene from Bacillus amyloliquefaciens. Gene 96: 89-93.
    • (1990) Gene , vol.96 , pp. 89-93
    • Tang, L.B.1    Lenstra, R.2    Borchert, T.V.3    Nagarajan, V.4
  • 21
    • 27644486636 scopus 로고    scopus 로고
    • Determination of the g-matrix orientation in flavin radicals by high-rield/high-frequency electronnuclear double resonance
    • Weber S, Kay CWM, Schleicher E, Hitomi K, Todo T, et al. (2005) Determination of the g-matrix orientation in flavin radicals by high-rield/high-frequency electronnuclear double resonance. Magnetic Resonance in Chemistry 43: S96-S102.
    • (2005) Magnetic Resonance in Chemistry , vol.43
    • Weber, S.1    Kay, C.W.M.2    Schleicher, E.3    Hitomi, K.4    Todo, T.5
  • 24
    • 33947527046 scopus 로고    scopus 로고
    • Biochemistry: molecular cannibalism
    • Ealick S, Begley T, (2007) Biochemistry: molecular cannibalism. Nature London 446: 387.
    • (2007) Nature London , vol.446 , pp. 387
    • Ealick, S.1    Begley, T.2
  • 25
    • 79952774271 scopus 로고    scopus 로고
    • Intermediate-Assisted Multifunctional Catalysis in the Conversion of Flavin to 5,6-Dimethylbenzimidazole by BluB: A Density Functional Theory Study
    • Quan JM, Wang XL, (2011) Intermediate-Assisted Multifunctional Catalysis in the Conversion of Flavin to 5,6-Dimethylbenzimidazole by BluB: A Density Functional Theory Study. Journal of the American Chemical Society 133: 4079-4091.
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 4079-4091
    • Quan, J.M.1    Wang, X.L.2
  • 26
    • 71149117143 scopus 로고    scopus 로고
    • The Electronic State of Flavoproteins: Investigations with Proton Electron-Nuclear Double Resonance
    • Weber S, Schleicher E, Wenzel R, Ahmad M, Batschauer A, et al. (2010) The Electronic State of Flavoproteins: Investigations with Proton Electron-Nuclear Double Resonance. Applied Magnetic Resonance 37: 339-352.
    • (2010) Applied Magnetic Resonance , vol.37 , pp. 339-352
    • Weber, S.1    Schleicher, E.2    Wenzel, R.3    Ahmad, M.4    Batschauer, A.5
  • 27
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: sequence, folding, binding, function and beyond
    • Sancho J, (2006) Flavodoxins: sequence, folding, binding, function and beyond. Cellular and Molecular Life Sciences 63: 855-864.
    • (2006) Cellular and Molecular Life Sciences , vol.63 , pp. 855-864
    • Sancho, J.1
  • 28
    • 19944434206 scopus 로고    scopus 로고
    • Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors
    • McGoldrick H, Roessner C, Raux E, Lawrence A, McLean K, et al. (2005) Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors. Journal of Biological Chemistry 280: 1086.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 1086
    • McGoldrick, H.1    Roessner, C.2    Raux, E.3    Lawrence, A.4    McLean, K.5
  • 29
    • 44849134910 scopus 로고    scopus 로고
    • Identification, characterization, and structure/function analysis of a corrin reductase involved in adenosylcobalamin biosynthesis
    • Lawrence AD, Deery E, McLean KJ, Munro AW, Pickersgill RW, et al. (2008) Identification, characterization, and structure/function analysis of a corrin reductase involved in adenosylcobalamin biosynthesis. Journal of Biological Chemistry 283: 10813.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 10813
    • Lawrence, A.D.1    Deery, E.2    McLean, K.J.3    Munro, A.W.4    Pickersgill, R.W.5
  • 30
    • 0013954466 scopus 로고
    • On the Existence of Spectrally Distinct Classes of Flavoprotein Semiquinones. A New Method for the Quantitative Production of Flavoprotein Semiquinones*
    • Massey V, Palmer G, (1966) On the Existence of Spectrally Distinct Classes of Flavoprotein Semiquinones. A New Method for the Quantitative Production of Flavoprotein Semiquinones*. Biochemistry 5: 3181-3189.
    • (1966) Biochemistry , vol.5 , pp. 3181-3189
    • Massey, V.1    Palmer, G.2
  • 31
    • 0014669476 scopus 로고
    • Purification and characterization of flavodoxin from Peptostreptococcus elsdenii
    • Mayhew S, Massey V, (1969) Purification and characterization of flavodoxin from Peptostreptococcus elsdenii. Journal of Biological Chemistry 244: 794.
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 794
    • Mayhew, S.1    Massey, V.2
  • 32
    • 18844474423 scopus 로고    scopus 로고
    • Potentiometric Analysis of the Flavin Cofactors of Neuronal Nitric Oxide Synthase†
    • Noble M, Munro A, Rivers S, Robledo L, Daff S, et al. (1999) Potentiometric Analysis of the Flavin Cofactors of Neuronal Nitric Oxide Synthase†. Biochemistry 38: 16413-16418.
    • (1999) Biochemistry , vol.38 , pp. 16413-16418
    • Noble, M.1    Munro, A.2    Rivers, S.3    Robledo, L.4    Daff, S.5
  • 33
    • 45549089089 scopus 로고    scopus 로고
    • The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B-12 synthesis
    • Bobik TA, Fan CG, (2008) The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B-12 synthesis. Journal of Biological Chemistry 283: 11322-11329.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 11322-11329
    • Bobik, T.A.1    Fan, C.G.2
  • 34
    • 0004136246 scopus 로고    scopus 로고
    • Sambrook J, Russell DW, editors. Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press
    • Sambrook J, Russell DW (2001) Molecular Cloning: A laboratory manual; Sambrook J, Russell DW, editors. Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press. 999 p.
    • (2001) Molecular Cloning: A laboratory manual , pp. 999
    • Sambrook, J.1    Russell, D.W.2
  • 35
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4
    • Läemmli UK, (1970) Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Läemmli, U.K.1
  • 36
    • 0018115502 scopus 로고
    • Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton P, (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods in Enzymology 54: 411.
    • (1978) Methods in Enzymology , vol.54 , pp. 411
    • Dutton, P.1
  • 37
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK, (2001) Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 40: 1956-1963.
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 38
    • 0037426330 scopus 로고    scopus 로고
    • Molecular dissection of human methionine synthase reductase: Determination of the flavin redox potentials in full-length enzyme and isolated flavin-binding domains
    • Scrutton NS, Wolthers KR, Basran J, Munro AW, (2003) Molecular dissection of human methionine synthase reductase: Determination of the flavin redox potentials in full-length enzyme and isolated flavin-binding domains. Biochemistry 42: 3911-3920.
    • (2003) Biochemistry , vol.42 , pp. 3911-3920
    • Scrutton, N.S.1    Wolthers, K.R.2    Basran, J.3    Munro, A.W.4
  • 40
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel HJ, Bonner DM, (1956) Acetylornithinase of Escherichia coli: partial purification and some properties. Journal of Biological Chemistry 218: 97-106.
    • (1956) Journal of Biological Chemistry , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 41
    • 0017030513 scopus 로고
    • New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressureized atmosphere
    • Balch WE, Wolfe RS, (1976) New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressureized atmosphere. Applied Environmental Microbiology 32: 781-791.
    • (1976) Applied Environmental Microbiology , vol.32 , pp. 781-791
    • Balch, W.E.1    Wolfe, R.S.2
  • 42
    • 0001679071 scopus 로고
    • Selected topics from classical bacterial genetics
    • In: Ausubel FA, Brent R, Kingston RE, Moore DD, Seidman JG et al., editors. New York: Wiley Interscience
    • Raleigh EA, Lech K, Brent R (1989) Selected topics from classical bacterial genetics. In: Ausubel FA, Brent R, Kingston RE, Moore DD, Seidman JG et al., editors. Current Protocols in Molecular Biology. New York: Wiley Interscience. pp. p. 1.4.
    • (1989) Current Protocols in Molecular Biology
    • Raleigh, E.A.1    Lech, K.2    Brent, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.