메뉴 건너뛰기




Volumn 20, Issue 6, 2010, Pages 673-683

Substrate activation by iron superoxo intermediates

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYETHYLPHOSPHONIC ACID DIOXYGENASE; CARBON; DIOXYGENASE; HYDROGEN; INOSITOL OXYGENASE; IRON SUPEROXIDE DISMUTASE; ISOPENICILLIN N SYNTHETASE; NONHEME IRON PROTEIN; UNCLASSIFIED DRUG;

EID: 78649675114     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.08.005     Document Type: Review
Times cited : (101)

References (51)
  • 2
    • 34047141801 scopus 로고    scopus 로고
    • Enzymatic C-H activation by metal-superoxo intermediates
    • Bollinger J.M., Krebs C. Enzymatic C-H activation by metal-superoxo intermediates. Curr Opin Chem Biol 2007, 11:151-158.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 151-158
    • Bollinger, J.M.1    Krebs, C.2
  • 4
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que L., Ho R.Y.N. Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 1996, 96:2607-2624.
    • (1996) Chem Rev , vol.96 , pp. 2607-2624
    • Que, L.1    Ho, R.Y.N.2
  • 5
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
    • Kovaleva E.G., Lipscomb J.D. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat Chem Biol 2008, 4:186-193.
    • (2008) Nat Chem Biol , vol.4 , pp. 186-193
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 6
    • 4644302003 scopus 로고    scopus 로고
    • The oxo/peroxo debate: a nonheme iron perspective
    • Que L. The oxo/peroxo debate: a nonheme iron perspective. J Biol Inorg Chem 2004, 9:684-690.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 684-690
    • Que, L.1
  • 7
    • 0000502480 scopus 로고
    • Isopenicillin N synthase: mechanistic studies
    • Baldwin J.E., Bradley M. Isopenicillin N synthase: mechanistic studies. Chem Rev 1990, 90:1079-1088.
    • (1990) Chem Rev , vol.90 , pp. 1079-1088
    • Baldwin, J.E.1    Bradley, M.2
  • 9
    • 4243616042 scopus 로고
    • Principles of structure, bonding, and reactivity for metal nitrosyl complexes
    • Enemark J.H., Feltham R.D. Principles of structure, bonding, and reactivity for metal nitrosyl complexes. Coord Chem Rev 1974, 13:339-406.
    • (1974) Coord Chem Rev , vol.13 , pp. 339-406
    • Enemark, J.H.1    Feltham, R.D.2
  • 10
    • 34250883989 scopus 로고    scopus 로고
    • 8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in nonheme Fe enzymes
    • 8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in nonheme Fe enzymes. J Am Chem Soc 2007, 129:7427-7438.
    • (2007) J Am Chem Soc , vol.129 , pp. 7427-7438
    • Brown, C.D.1    Neidig, M.L.2    Neibergall, M.B.3    Lipscomb, J.D.4    Solomon, E.I.5
  • 14
    • 0041732088 scopus 로고    scopus 로고
    • CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis
    • Pojer F., Kahlich R., Kammerer B., Li S.M., Heide L. CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis. J Biol Chem 2003, 278:30661-30668.
    • (2003) J Biol Chem , vol.278 , pp. 30661-30668
    • Pojer, F.1    Kahlich, R.2    Kammerer, B.3    Li, S.M.4    Heide, L.5
  • 15
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J., Hajdu J., Baldwin J.E. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 1997, 387:827-830.
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 16
    • 33845560175 scopus 로고
    • Theoretical studies of the oxy anionic substituent effect
    • Steigerwald M.L., Goddard W.A., Evans D.A. Theoretical studies of the oxy anionic substituent effect. J Am Chem Soc 1979, 101:1994-1997.
    • (1979) J Am Chem Soc , vol.101 , pp. 1994-1997
    • Steigerwald, M.L.1    Goddard, W.A.2    Evans, D.A.3
  • 19
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins
    • Merkx M., Kopp D.A., Sazinsky M.H., Blazyk J.L., Müller J., Lippard S.J. Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins. Angew Chem Int Ed Engl 2001, 40:2782-2807.
    • (2001) Angew Chem Int Ed Engl , vol.40 , pp. 2782-2807
    • Merkx, M.1    Kopp, D.A.2    Sazinsky, M.H.3    Blazyk, J.L.4    Müller, J.5    Lippard, S.J.6
  • 20
    • 33646347856 scopus 로고    scopus 로고
    • Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo-inositol oxygenase
    • Xing G., Barr E.W., Diao Y., Hoffart L.M., Prabhu K.S., Arner R.J., Reddy C.C., Krebs C., Bollinger J.M. Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo-inositol oxygenase. Biochemistry 2006, 45:5402-5412.
    • (2006) Biochemistry , vol.45 , pp. 5402-5412
    • Xing, G.1    Barr, E.W.2    Diao, Y.3    Hoffart, L.M.4    Prabhu, K.S.5    Arner, R.J.6    Reddy, C.C.7    Krebs, C.8    Bollinger, J.M.9
  • 22
    • 70350489461 scopus 로고    scopus 로고
    • Lipoxygenases-structure and reaction mechanism
    • Andreou A., Feussner I. Lipoxygenases-structure and reaction mechanism. Phytochemistry 2009, 70:1504-1510.
    • (2009) Phytochemistry , vol.70 , pp. 1504-1510
    • Andreou, A.1    Feussner, I.2
  • 23
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman M.H., Klinman J.P. Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover. Biochemistry 1996, 35:12882-12892.
    • (1996) Biochemistry , vol.35 , pp. 12882-12892
    • Glickman, M.H.1    Klinman, J.P.2
  • 24
    • 70349278483 scopus 로고    scopus 로고
    • FtmOx1, a non-heme Fe(II) and alpha-ketoglutarate-dependent dioxygenase, catalyses the endoperoxide formation of verruculogen in Aspergillus fumigatus
    • Steffan N., Grundmann A., Afiyatullov S., Ruan H., Li S.M. FtmOx1, a non-heme Fe(II) and alpha-ketoglutarate-dependent dioxygenase, catalyses the endoperoxide formation of verruculogen in Aspergillus fumigatus. Org Biomol Chem 2009, 7:4082-4087.
    • (2009) Org Biomol Chem , vol.7 , pp. 4082-4087
    • Steffan, N.1    Grundmann, A.2    Afiyatullov, S.3    Ruan, H.4    Li, S.M.5
  • 25
    • 27144467824 scopus 로고    scopus 로고
    • Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme
    • Higgins L.J., Yan F., Liu P., Liu H.W., Drennan C.L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 2005, 437:838-844.
    • (2005) Nature , vol.437 , pp. 838-844
    • Higgins, L.J.1    Yan, F.2    Liu, P.3    Liu, H.W.4    Drennan, C.L.5
  • 26
    • 0343986411 scopus 로고    scopus 로고
    • One motif-many different reactions
    • Que L. One motif-many different reactions. Nature Struct Biol 2000, 7:182-184.
    • (2000) Nature Struct Biol , vol.7 , pp. 182-184
    • Que, L.1
  • 27
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • Koehntop K.D., Emerson J.P., Que L. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J Biol Inorg Chem 2005, 10:87-93.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que, L.3
  • 28
    • 70450208557 scopus 로고    scopus 로고
    • Hydroperoxylation by hydroxyethylphosphonate dioxygenase
    • Whitteck J.T., Cicchillo R.M., van der Donk W.A. Hydroperoxylation by hydroxyethylphosphonate dioxygenase. J Am Chem Soc 2009, 131:16225-16232.
    • (2009) J Am Chem Soc , vol.131 , pp. 16225-16232
    • Whitteck, J.T.1    Cicchillo, R.M.2    van der Donk, W.A.3
  • 29
    • 0000253950 scopus 로고
    • Acyl phosphates from acyl phosphonates-a novel Baeyer-Villiger rearrangement
    • Gordon N.J., Evans S.A. Acyl phosphates from acyl phosphonates-a novel Baeyer-Villiger rearrangement. J Org Chem 1993, 58:4516-4519.
    • (1993) J Org Chem , vol.58 , pp. 4516-4519
    • Gordon, N.J.1    Evans, S.A.2
  • 31
    • 29644433009 scopus 로고    scopus 로고
    • Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism
    • Koehntop K.D., Marimanikkuppam S., Ryle M.J., Hausinger R.P., Que L. Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism. J Biol Inorg Chem 2006, 11:63-72.
    • (2006) J Biol Inorg Chem , vol.11 , pp. 63-72
    • Koehntop, K.D.1    Marimanikkuppam, S.2    Ryle, M.J.3    Hausinger, R.P.4    Que, L.5
  • 32
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger R.P. Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes. Crit Rev Biochem Mol Biol 2004, 39:21-68.
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 33
    • 33749542309 scopus 로고    scopus 로고
    • Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase
    • Hoffart L.M., Barr E.W., Guyer R.B., Bollinger J.M., Krebs C. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. Proc Natl Acad Sci U S A 2006, 103:14738-14743.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14738-14743
    • Hoffart, L.M.1    Barr, E.W.2    Guyer, R.B.3    Bollinger, J.M.4    Krebs, C.5
  • 34
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • Price J.C., Barr E.W., Tirupati B., Bollinger J.M., Krebs C. The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 2003, 42:7497-7508.
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger, J.M.4    Krebs, C.5
  • 35
    • 0142183453 scopus 로고    scopus 로고
    • Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:alpha-ketoglutarate dioxygenase (TauD)
    • Price J.C., Barr E.W., Glass T.E., Krebs C., Bollinger J.M. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:alpha-ketoglutarate dioxygenase (TauD). J Am Chem Soc 2003, 125:13008-13009.
    • (2003) J Am Chem Soc , vol.125 , pp. 13008-13009
    • Price, J.C.1    Barr, E.W.2    Glass, T.E.3    Krebs, C.4    Bollinger, J.M.5
  • 36
    • 33748359090 scopus 로고    scopus 로고
    • Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes
    • Neidig M.L., Decker A., Choroba O.W., Huang F., Kavana M., Moran G.R., Spencer J.B., Solomon E.I. Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes. Proc Natl Acad Sci U S A 2006, 103:12966-12973.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12966-12973
    • Neidig, M.L.1    Decker, A.2    Choroba, O.W.3    Huang, F.4    Kavana, M.5    Moran, G.R.6    Spencer, J.B.7    Solomon, E.I.8
  • 37
    • 77949355783 scopus 로고    scopus 로고
    • Oxidative decarboxylation of alpha-hydroxy acids by a functional model of the nonheme iron oxygenase, CloR
    • Paine T.K., Paria S., Que L. Oxidative decarboxylation of alpha-hydroxy acids by a functional model of the nonheme iron oxygenase, CloR. Chem Commun 2010, 46:1830-1832.
    • (2010) Chem Commun , vol.46 , pp. 1830-1832
    • Paine, T.K.1    Paria, S.2    Que, L.3
  • 38
    • 70349560007 scopus 로고    scopus 로고
    • Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue
    • Ge W., Clifton I.J., Howard-Jones A.R., Stok J.E., Adlington R.M., Baldwin J.E., Rutledge P.J. Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue. ChemBioChem 2009, 10:2025-2031.
    • (2009) ChemBioChem , vol.10 , pp. 2025-2031
    • Ge, W.1    Clifton, I.J.2    Howard-Jones, A.R.3    Stok, J.E.4    Adlington, R.M.5    Baldwin, J.E.6    Rutledge, P.J.7
  • 39
    • 76749129792 scopus 로고    scopus 로고
    • Reaction coordinate of isopenicillin N synthase: oxidase versus oxygenase activity
    • Brown-Marshall C.D., Diebold A.R., Solomon E.I. Reaction coordinate of isopenicillin N synthase: oxidase versus oxygenase activity. Biochemistry 2010, 49:1176-1182.
    • (2010) Biochemistry , vol.49 , pp. 1176-1182
    • Brown-Marshall, C.D.1    Diebold, A.R.2    Solomon, E.I.3
  • 40
    • 0008713567 scopus 로고
    • Biosynthesis of natural products with a P-C bond, part 8: on the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae
    • Hammerschmidt F. Biosynthesis of natural products with a P-C bond, part 8: on the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae. J Chem Soc Perkin Trans 1991, 1:1993-1996.
    • (1991) J Chem Soc Perkin Trans , vol.1 , pp. 1993-1996
    • Hammerschmidt, F.1
  • 41
    • 0034803518 scopus 로고    scopus 로고
    • Protein purification and function assignment of the epoxidase catalyzing the formation of fosfomycin
    • Liu P., Murakami K., Seki T., He X., Yeung S.M., Kuzuyama T., Seto H., Liu H.W. Protein purification and function assignment of the epoxidase catalyzing the formation of fosfomycin. J Am Chem Soc 2001, 123:4619-4620.
    • (2001) J Am Chem Soc , vol.123 , pp. 4619-4620
    • Liu, P.1    Murakami, K.2    Seki, T.3    He, X.4    Yeung, S.M.5    Kuzuyama, T.6    Seto, H.7    Liu, H.W.8
  • 42
    • 0037011396 scopus 로고    scopus 로고
    • Mechanistic studies of HPP epoxidase: configuration of the substrate governs its enzymatic fate
    • Zhao Z., Liu P., Murakami K., Kuzuyama T., Seto H., Liu H.W. Mechanistic studies of HPP epoxidase: configuration of the substrate governs its enzymatic fate. Angew Chem, Int Ed Engl 2002, 41:4529-4532.
    • (2002) Angew Chem, Int Ed Engl , vol.41 , pp. 4529-4532
    • Zhao, Z.1    Liu, P.2    Murakami, K.3    Kuzuyama, T.4    Seto, H.5    Liu, H.W.6
  • 43
    • 0141885319 scopus 로고    scopus 로고
    • Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme
    • Liu P., Liu A., Yan F., Wolfe M.D., Lipscomb J.D., Liu H.W. Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme. Biochemistry 2003, 42:11577-11586.
    • (2003) Biochemistry , vol.42 , pp. 11577-11586
    • Liu, P.1    Liu, A.2    Yan, F.3    Wolfe, M.D.4    Lipscomb, J.D.5    Liu, H.W.6
  • 46
    • 0032481388 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate
    • Pavel E.G., Zhou J., Busby R.W., Gunsior M., Townsend C.A., Solomon E.I. Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate. J Am Chem Soc 1998, 120:743-775.
    • (1998) J Am Chem Soc , vol.120 , pp. 743-775
    • Pavel, E.G.1    Zhou, J.2    Busby, R.W.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 49
    • 33750074424 scopus 로고    scopus 로고
    • Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism
    • Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., Loomes K.M., Baker E.N. Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism. Proc Natl Acad Sci U S A 2006, 103:15032-15037.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15032-15037
    • Brown, P.M.1    Caradoc-Davies, T.T.2    Dickson, J.M.3    Cooper, G.J.4    Loomes, K.M.5    Baker, E.N.6
  • 51
    • 77955401788 scopus 로고    scopus 로고
    • Dioxygen activation by a non-heme iron(II) complex: formation of an iron(IV)-oxo complex via C-H activation by a putative iron(III)-superoxo species
    • Lee Y.M., Hong S., Morimoto Y., Shin W., Fukuzumi S., Nam W. Dioxygen activation by a non-heme iron(II) complex: formation of an iron(IV)-oxo complex via C-H activation by a putative iron(III)-superoxo species. J Am Chem Soc 2010, 132:10668-10670.
    • (2010) J Am Chem Soc , vol.132 , pp. 10668-10670
    • Lee, Y.M.1    Hong, S.2    Morimoto, Y.3    Shin, W.4    Fukuzumi, S.5    Nam, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.