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Volumn 108, Issue 41, 2011, Pages 16956-16961

Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

Author keywords

Cytochrome; Electron hopping; Peroxidase; Protein oxidation; Protein radical

Indexed keywords

AMINE DEHYDROGENASE; ENZYME; IRON; MAUG ENZYME; QUINONE DERIVATIVE; TRYPTOPHAN; TRYPTOPHAN 199; TRYPTOPHAN TRYPTOPHYLQUINONE; UNCLASSIFIED DRUG;

EID: 80054742096     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1109423108     Document Type: Article
Times cited : (59)

References (37)
  • 1
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page CC, Moser CC, Chen X, Dutton PL (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402:47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 2
    • 47249166440 scopus 로고    scopus 로고
    • Control of true, gated, and coupled electron transfer reactions
    • Davidson VL (2008) Control of true, gated, and coupled electron transfer reactions. Acc Chem Res 41:730-738.
    • (2008) Acc Chem Res , vol.41 , pp. 730-738
    • Davidson, V.L.1
  • 3
    • 72449133054 scopus 로고    scopus 로고
    • Steering electrons on moving pathways
    • Beratan DN, et al. (2009) Steering electrons on moving pathways. Acc Chem Res 42:1669-1678.
    • (2009) Acc Chem Res , vol.42 , pp. 1669-1678
    • Beratan, D.N.1
  • 4
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • DOI 10.1017/S0033583503003913
    • Gray HB, Winkler JR (2003) Electron tunneling through proteins. Q Rev Biophys 36:341-372. (Pubitemid 38268661)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.3 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 5
    • 0029806796 scopus 로고    scopus 로고
    • Unraveling the kinetic complexity of interprotein electron transfer reactions
    • Davidson VL (1996) Unraveling the kinetic complexity of interprotein electron transfer reactions. Biochemistry 35:14035-14039.
    • (1996) Biochemistry , vol.35 , pp. 14035-14039
    • Davidson, V.L.1
  • 6
    • 0033975320 scopus 로고    scopus 로고
    • What controls the rates of interprotein electron-transfer reactions
    • Davidson VL (2000) What controls the rates of interprotein electron-transfer reactions. Acc Chem Res 33:87-93.
    • (2000) Acc Chem Res , vol.33 , pp. 87-93
    • Davidson, V.L.1
  • 7
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • DOI 10.1021/ja001278u
    • Baldwin J, et al. (2000) Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical. J Am Chem Soc 122:12195-12206. (Pubitemid 32062257)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.49 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 8
    • 73149099389 scopus 로고    scopus 로고
    • Use of 3-aminotyrosine to examine the pathway dependence of radical propagation in Escherichia coli ribonucleotide reductase
    • Minnihan EC, Seyedsayamdost MR, Stubbe J (2009) Use of 3-aminotyrosine to examine the pathway dependence of radical propagation in Escherichia coli ribonucleotide reductase. Biochemistry 48:12125-12132.
    • (2009) Biochemistry , vol.48 , pp. 12125-12132
    • Minnihan, E.C.1    Seyedsayamdost, M.R.2    Stubbe, J.3
  • 9
    • 55549100984 scopus 로고    scopus 로고
    • Electron hopping through the 15 A triple tryptophan molecular wire in DNA photolyase occurs within 30 ps
    • Lukacs A, Eker AP, Byrdin M, Brettel K, Vos MH (2008) Electron hopping through the 15 A triple tryptophan molecular wire in DNA photolyase occurs within 30 ps. J Am Chem Soc 130:14394-14395.
    • (2008) J Am Chem Soc , vol.130 , pp. 14394-14395
    • Lukacs, A.1    Eker, A.P.2    Byrdin, M.3    Brettel, K.4    Vos, M.H.5
  • 10
    • 57549111042 scopus 로고    scopus 로고
    • Electron transfer in peptides and proteins
    • Giese B, Graber M, Cordes M (2008) Electron transfer in peptides and proteins. Curr Opin Chem Biol 12:755-759.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 755-759
    • Giese, B.1    Graber, M.2    Cordes, M.3
  • 12
    • 0034797851 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase
    • Davidson VL (2001) Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase. Adv Protein Chem 58:95-140.
    • (2001) Adv Protein Chem , vol.58 , pp. 95-140
    • Davidson, V.L.1
  • 15
    • 33750702163 scopus 로고    scopus 로고
    • Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis
    • DOI 10.1021/bi061497d
    • Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL (2006) Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry 45:13276-13283. (Pubitemid 44707687)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13276-13283
    • Li, X.1    Jones, L.H.2    Pearson, A.R.3    Wilmot, C.M.4    Davidson, V.L.5
  • 16
    • 77949400738 scopus 로고    scopus 로고
    • In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex
    • Jensen LM, Sanishvili R, Davidson VL, Wilmot CM (2010) In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex. Science 327:1392-1394.
    • (2010) Science , vol.327 , pp. 1392-1394
    • Jensen, L.M.1    Sanishvili, R.2    Davidson, V.L.3    Wilmot, C.M.4
  • 17
    • 0025907553 scopus 로고
    • Structural microheterogeneity of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P-450cam
    • Stayton PS, Sligar SG (1991) Structural microheterogeneity of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P-450cam. Biochemistry 30:1845-1851.
    • (1991) Biochemistry , vol.30 , pp. 1845-1851
    • Stayton, P.S.1    Sligar, S.G.2
  • 19
    • 0027231963 scopus 로고
    • The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
    • Goodin DB, McRee DE (1993) The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry 32:3313-3324. (Pubitemid 23126897)
    • (1993) Biochemistry , vol.32 , Issue.13 , pp. 3313-3324
    • Goodin, D.B.1    McRee, D.E.2
  • 20
    • 0023411201 scopus 로고
    • Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin
    • Henry ER, Hochstrasser RM (1987) Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin. Proc Natl Acad Sci USA 84:6142-6146.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6142-6146
    • Henry, E.R.1    Hochstrasser, R.M.2
  • 21
    • 67650545661 scopus 로고    scopus 로고
    • Distinct role of specific tryptophans in facilitating electron transfer or as [Fe(IV) = OTrp(*)] intermediates in the peroxidase reaction of Bulkholderia pseudomallei catalase-peroxidase: A multifrequency EPR spectroscopy investigation
    • Colin J, Wiseman B, Switala J, Loewen PC, Ivancich A (2009) Distinct role of specific tryptophans in facilitating electron transfer or as [Fe(IV) = OTrp(*)] intermediates in the peroxidase reaction of Bulkholderia pseudomallei catalase-peroxidase: A multifrequency EPR spectroscopy investigation. J Am Chem Soc 131:8557-8563.
    • (2009) J Am Chem Soc , vol.131 , pp. 8557-8563
    • Colin, J.1    Wiseman, B.2    Switala, J.3    Loewen, P.C.4    Ivancich, A.5
  • 23
    • 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
    • DOI 10.1021/bi052000n
    • Li X, Feng M, Wang Y, Tachikawa H, Davidson VL (2006) Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis. Biochemistry 45:821-828. (Pubitemid 43122246)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 821-828
    • Li, X.1    Feng, M.2    Wang, Y.3    Tachikawa, H.4    Davidson, V.L.5
  • 24
    • 78650867534 scopus 로고    scopus 로고
    • The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis
    • Shin S, et al. (2011) The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis. Biochemistry 50:144-150.
    • (2011) Biochemistry , vol.50 , pp. 144-150
    • Shin, S.1
  • 25
    • 64849088182 scopus 로고    scopus 로고
    • Kinetic mechanism for the initial steps in MauGdependent tryptophan tryptophylquinone biosynthesis
    • Lee S, Shin S, Li X, Davidson VL (2009) Kinetic mechanism for the initial steps in MauGdependent tryptophan tryptophylquinone biosynthesis. Biochemistry 48:2442-2447.
    • (2009) Biochemistry , vol.48 , pp. 2442-2447
    • Lee, S.1    Shin, S.2    Li, X.3    Davidson, V.L.4
  • 26
    • 70350238504 scopus 로고    scopus 로고
    • 2in the absence of its natural protein substrate
    • 2 in the absence of its natural protein substrate. Biochemistry 48:10106-10112.
    • (2009) Biochemistry , vol.48 , pp. 10106-10112
    • Shin, S.1    Lee, S.2    Davidson, V.L.3
  • 27
    • 77954730201 scopus 로고    scopus 로고
    • Long range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase
    • Shin S, Abu Tarboush N, Davidson VL (2010) Long range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase. Biochemistry 49:5810-5816.
    • (2010) Biochemistry , vol.49 , pp. 5810-5816
    • Shin, S.1    Abu Tarboush, N.2    Davidson, V.L.3
  • 30
    • 33748652072 scopus 로고    scopus 로고
    • Reduction potential of histidine free radicals: A pulse radiolysis study
    • Navarathnam S, Parsons BJ (1998) Reduction potential of histidine free radicals: A pulse radiolysis study. J Chem Soc Faraday Trans 94:2577-2581.
    • (1998) J Chem Soc Faraday Trans , vol.94 , pp. 2577-2581
    • Navarathnam, S.1    Parsons, B.J.2
  • 33
    • 0024384199 scopus 로고
    • Pulse radiolytic measurement of redox potentials: The tyrosine and tryptophan radicals
    • DOI 10.1021/bi00437a049
    • DeFelippis MR, Murthy CP, Faraggi M, Klapper MH (1989) Pulse radiolytic measurement of redox potentials: The tyrosine and tryptophan radicals. Biochemistry 28:4847-4853. (Pubitemid 19151066)
    • (1989) Biochemistry , vol.28 , Issue.11 , pp. 4847-4853
    • DeFelippis, M.R.1    Murthy, C.P.2    Faraggi, M.3    Klapper, M.H.4
  • 34
    • 0000947245 scopus 로고
    • Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks HB, Davidson VL (1994) Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin. J Am Chem Soc 116:11201-11202.
    • (1994) J Am Chem Soc , vol.116 , pp. 11201-11202
    • Brooks, H.B.1    Davidson, V.L.2
  • 35
    • 0025026513 scopus 로고
    • Methylamine dehydrogenases from methylotrophic bacteria
    • Davidson VL (1990) Methylamine dehydrogenases from methylotrophic bacteria. Methods Enzymol 188:241-246.
    • (1990) Methods Enzymol , vol.188 , pp. 241-246
    • Davidson, V.L.1
  • 37
    • 40149106660 scopus 로고    scopus 로고
    • Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone
    • DOI 10.1021/bi702259w
    • Li X, Fu R, Liu A, Davidson VL (2008) Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry 47:2908-2912. (Pubitemid 351328843)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2908-2912
    • Li, X.1    Fu, R.2    Liu, A.3    Davidson, V.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.