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Volumn 1824, Issue 11, 2012, Pages 1299-1305

Tryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational modification

Author keywords

Cytochrome; Electron transfer; Ferryl intermediate; Heme; MauG; Methylamine dehydrogenase

Indexed keywords

AMINE DEHYDROGENASE; FERROUS ION; HEME; OXYGEN; QUINONE DERIVATIVE; TRYPTOPHAN DERIVATIVE; TRYPTOPHAN TRYPTOPHYLQUINONE; UNCLASSIFIED DRUG;

EID: 84866017724     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.01.008     Document Type: Review
Times cited : (13)

References (35)
  • 1
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • W.S. McIntire, D.E. Wemmer, A. Chistoserdov, and M.E. Lidstrom A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase Science 252 1991 817 824
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S.1    Wemmer, D.E.2    Chistoserdov, A.3    Lidstrom, M.E.4
  • 2
    • 34248189231 scopus 로고    scopus 로고
    • Protein-derived cofactors. Expanding the scope of post-translational modifications
    • V.L. Davidson Protein-derived cofactors. Expanding the scope of post-translational modifications Biochemistry 46 2007 5283 5292
    • (2007) Biochemistry , vol.46 , pp. 5283-5292
    • Davidson, V.L.1
  • 3
    • 78650157270 scopus 로고    scopus 로고
    • Generation of protein-derived redox cofactors by posttranslational modification
    • V.L. Davidson Generation of protein-derived redox cofactors by posttranslational modification Mol. Biosyst. 7 2011 29 37
    • (2011) Mol. Biosyst. , vol.7 , pp. 29-37
    • Davidson, V.L.1
  • 4
    • 0034797851 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase
    • V.L. Davidson Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase Adv. Protein Chem. 58 2001 95 140
    • (2001) Adv. Protein Chem. , vol.58 , pp. 95-140
    • Davidson, V.L.1
  • 5
    • 0027481125 scopus 로고
    • Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 Å and 1.8 Å resolution
    • R. Durley, L. Chen, L.W. Lim, F.S. Mathews, and V.L. Davidson Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 Å and 1.8 Å resolution Protein Sci. 2 1993 739 752
    • (1993) Protein Sci. , vol.2 , pp. 739-752
    • Durley, R.1    Chen, L.2    Lim, L.W.3    Mathews, F.S.4    Davidson, V.L.5
  • 6
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role
    • M. Husain, and V.L. Davidson An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role J. Biol. Chem. 260 1985 14626 14629
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 9
    • 0028296944 scopus 로고
    • Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin, and cytochrome c551i
    • L. Chen, R.C. Durley, F.S. Mathews, and V.L. Davidson Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i Science 264 1994 86 90
    • (1994) Science , vol.264 , pp. 86-90
    • Chen, L.1    Durley, R.C.2    Mathews, F.S.3    Davidson, V.L.4
  • 10
    • 0026720414 scopus 로고
    • The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans
    • A.Y. Chistoserdov, J. Boyd, F.S. Mathews, and M.E. Lidstrom The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans Biochem. Biophys. Res. Commun. 184 1992 1181 1189
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1181-1189
    • Chistoserdov, A.Y.1    Boyd, J.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 12
    • 0025149403 scopus 로고
    • Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation
    • R.J. van Spanning, C.W. Wansell, W.N. Reijnders, L.F. Oltmann, and A.H. Stouthamer Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation FEBS Lett. 275 1990 217 220
    • (1990) FEBS Lett. , vol.275 , pp. 217-220
    • Van Spanning, R.J.1    Wansell, C.W.2    Reijnders, W.N.3    Oltmann, L.F.4    Stouthamer, A.H.5
  • 16
    • 33750702163 scopus 로고    scopus 로고
    • Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis
    • X. Li, L.H. Jones, A.R. Pearson, C.M. Wilmot, and V.L. Davidson Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis Biochemistry 45 2006 13276 13283
    • (2006) Biochemistry , vol.45 , pp. 13276-13283
    • Li, X.1    Jones, L.H.2    Pearson, A.R.3    Wilmot, C.M.4    Davidson, V.L.5
  • 17
    • 33749163547 scopus 로고    scopus 로고
    • Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase
    • A.R. Pearson, S. Marimanikkuppam, X. Li, V.L. Davidson, and C.M. Wilmot Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase J. Am. Chem. Soc. 128 2006 12416 12417
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12416-12417
    • Pearson, A.R.1    Marimanikkuppam, S.2    Li, X.3    Davidson, V.L.4    Wilmot, C.M.5
  • 18
    • 0038070331 scopus 로고    scopus 로고
    • MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis
    • Y. Wang, M.E. Graichen, A. Liu, A.R. Pearson, C.W. Wilmot, and V.L. Davidson MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis Biochemistry 42 2003 7318 7325
    • (2003) Biochemistry , vol.42 , pp. 7318-7325
    • Wang, Y.1    Graichen, M.E.2    Liu, A.3    Pearson, A.R.4    Wilmot, C.W.5    Davidson, V.L.6
  • 19
    • 77949400738 scopus 로고    scopus 로고
    • In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex
    • L.M. Jensen, R. Sanishvili, V.L. Davidson, and C.M. Wilmot In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex Science 327 2010 1392 1394
    • (2010) Science , vol.327 , pp. 1392-1394
    • Jensen, L.M.1    Sanishvili, R.2    Davidson, V.L.3    Wilmot, C.M.4
  • 20
    • 31044447260 scopus 로고    scopus 로고
    • Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis
    • X. Li, M. Feng, Y. Wang, H. Tachikawa, and V.L. Davidson Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis Biochemistry 45 2006 821 828
    • (2006) Biochemistry , vol.45 , pp. 821-828
    • Li, X.1    Feng, M.2    Wang, Y.3    Tachikawa, H.4    Davidson, V.L.5
  • 21
    • 71549131616 scopus 로고    scopus 로고
    • Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands
    • R. Fu, F. Liu, V.L. Davidson, and A. Liu Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands Biochemistry 48 2009 11603 11605
    • (2009) Biochemistry , vol.48 , pp. 11603-11605
    • Fu, R.1    Liu, F.2    Davidson, V.L.3    Liu, A.4
  • 22
    • 79953683155 scopus 로고    scopus 로고
    • Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: Implications for the mechanism of dioxygen activation
    • E.T. Yukl, B.R. Goblirsch, V.L. Davidson, and C.M. Wilmot Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: Implications for the mechanism of dioxygen activation Biochemistry 50 2011 2931 2938
    • (2011) Biochemistry , vol.50 , pp. 2931-2938
    • Yukl, E.T.1    Goblirsch, B.R.2    Davidson, V.L.3    Wilmot, C.M.4
  • 23
    • 47249161981 scopus 로고    scopus 로고
    • A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical
    • X. Li, R. Fu, S. Lee, C. Krebs, V.L. Davidson, and A. Liu A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical Proc. Natl. Acad. Sci. U. S. A. 105 2008 8597 8600
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8597-8600
    • Li, X.1    Fu, R.2    Lee, S.3    Krebs, C.4    Davidson, V.L.5    Liu, A.6
  • 24
    • 77957905237 scopus 로고    scopus 로고
    • Unprecedented Fe(IV) species in a diheme protein MauG: A quantum chemical investigation on the unusual Mossbauer spectroscopic properties
    • Y. Ling, Y. Zhang, and V.L. Davidson Unprecedented Fe(IV) species in a diheme protein MauG: A quantum chemical investigation on the unusual Mossbauer spectroscopic properties J. Phys. Chem. Lett. 1 2010 2936 2939
    • (2010) J. Phys. Chem. Lett. , vol.1 , pp. 2936-2939
    • Ling, Y.1    Zhang, Y.2    Davidson, V.L.3
  • 25
    • 0037112289 scopus 로고    scopus 로고
    • Mössbauer investigations of the hexachlorantimonate salt of the phenyliron 2,3,7,8, l2,13,17,18-octaethyl-5,10,15,20-tetraphenylporphyrinate, [Fe(oetpp)Ph]SbCl6 and X-ray structure of the phenyliron(III) precursor Fe(III)(oetpp)Ph
    • E. Bill, V. Schunemann, A.X. Trautwein, R. Weiss, J. Fischer, A. Tabard, and R. Guilard Mössbauer investigations of the hexachlorantimonate salt of the phenyliron 2,3,7,8, l2,13,17,18-octaethyl-5,10,15,20- tetraphenylporphyrinate, [Fe(oetpp)Ph]SbCl6 and X-ray structure of the phenyliron(III) precursor Fe(III)(oetpp)Ph Inorg. Chim. Acta 339 2002 420 426
    • (2002) Inorg. Chim. Acta , vol.339 , pp. 420-426
    • Bill, E.1    Schunemann, V.2    Trautwein, A.X.3    Weiss, R.4    Fischer, J.5    Tabard, A.6    Guilard, R.7
  • 27
    • 0017133108 scopus 로고
    • Mössbauer spectroscopic study of Compound ES of cytochrome c peroxidase
    • G. Lang, K. Spartalian, and T. Yonetani Mössbauer spectroscopic study of Compound ES of cytochrome c peroxidase Biochim. Biophys. Acta 451 1976 250 258
    • (1976) Biochim. Biophys. Acta , vol.451 , pp. 250-258
    • Lang, G.1    Spartalian, K.2    Yonetani, T.3
  • 28
    • 0020534229 scopus 로고
    • Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase
    • P.S. Ho, B.M. Hoffman, C.H. Kang, and E. Margoliash Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase J. Biol. Chem. 258 1983 4356 4363
    • (1983) J. Biol. Chem. , vol.258 , pp. 4356-4363
    • Ho, P.S.1    Hoffman, B.M.2    Kang, C.H.3    Margoliash, E.4
  • 29
    • 78149421684 scopus 로고    scopus 로고
    • Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine
    • N. Abu Tarboush, L.M. Jensen, M. Feng, H. Tachikawa, C.M. Wilmot, and V.L. Davidson Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine Biochemistry 49 2010 9783 9791
    • (2010) Biochemistry , vol.49 , pp. 9783-9791
    • Abu Tarboush, N.1    Jensen, L.M.2    Feng, M.3    Tachikawa, H.4    Wilmot, C.M.5    Davidson, V.L.6
  • 31
    • 40149106660 scopus 로고    scopus 로고
    • Kinetic and physical evidence that the di-heme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone
    • X. Li, R. Fu, A. Liu, and V.L. Davidson Kinetic and physical evidence that the di-heme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone Biochemistry 47 2008 2908 2912
    • (2008) Biochemistry , vol.47 , pp. 2908-2912
    • Li, X.1    Fu, R.2    Liu, A.3    Davidson, V.L.4
  • 32
    • 77954730201 scopus 로고    scopus 로고
    • Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase
    • S. Shin, N. Abu Tarboush, and V.L. Davidson Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase Biochemistry 49 2010 5810 5816
    • (2010) Biochemistry , vol.49 , pp. 5810-5816
    • Shin, S.1    Abu Tarboush, N.2    Davidson, V.L.3
  • 33
    • 64849088182 scopus 로고    scopus 로고
    • Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis
    • S. Lee, S. Shin, X. Li, and V.L. Davidson Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis Biochemistry 48 2009 2442 2447
    • (2009) Biochemistry , vol.48 , pp. 2442-2447
    • Lee, S.1    Shin, S.2    Li, X.3    Davidson, V.L.4
  • 34
    • 4644275807 scopus 로고    scopus 로고
    • Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes
    • B. Meunier, S.P. de Visser, and S. Shaik Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes Chem. Rev. 104 2004 3947 3980
    • (2004) Chem. Rev. , vol.104 , pp. 3947-3980
    • Meunier, B.1    De Visser, S.P.2    Shaik, S.3


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