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Volumn 1787, Issue 9, 2009, Pages 1112-1121

Photo-catalytic oxidation of a di-nuclear manganese centre in an engineered bacterioferritin 'reaction centre'

Author keywords

Artificial photosynthesis; Bacterioferritin; Electron transfer; EPR; Manganese; Protein engineering; Zinc chlorin e6

Indexed keywords

BACTERIOFERRITIN; CHLORINE; FERRITIN; HEMOPROTEIN; IRON; MANGANESE; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 67649499951     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.04.011     Document Type: Article
Times cited : (43)

References (73)
  • 2
    • 57849138411 scopus 로고    scopus 로고
    • Designing Photosystem II: molecular engineering of photo-catalytic proteins
    • Conlan B. Designing Photosystem II: molecular engineering of photo-catalytic proteins. Photosyn. Res. 98 (2008) 687-700
    • (2008) Photosyn. Res. , vol.98 , pp. 687-700
    • Conlan, B.1
  • 4
    • 0032873285 scopus 로고    scopus 로고
    • Histidine placement in de novo-designed heme proteins
    • Gibney B.R., and Dutton P.L. Histidine placement in de novo-designed heme proteins. Protein Sci. 8 (1999) 1888-1898
    • (1999) Protein Sci. , vol.8 , pp. 1888-1898
    • Gibney, B.R.1    Dutton, P.L.2
  • 6
    • 67649571630 scopus 로고    scopus 로고
    • Molecular design as an approach to understanding membrane protein structure and function
    • DeGrado W.F. Molecular design as an approach to understanding membrane protein structure and function. FASEB J. 13 (1999) A1431
    • (1999) FASEB J. , vol.13
    • DeGrado, W.F.1
  • 8
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X.X., and Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402 (1999) 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 11
    • 0030744604 scopus 로고    scopus 로고
    • Electron tunneling in proteins: role of the intervening medium
    • Winkler J.R., and Gray H.B. Electron tunneling in proteins: role of the intervening medium. J. Biol. Inorg. Chem. 2 (1997) 399-404
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 399-404
    • Winkler, J.R.1    Gray, H.B.2
  • 12
    • 33645004855 scopus 로고    scopus 로고
    • Design and engineering of photosynthetic light-harvesting and electron transfer using length, time, and energy scales
    • Noy D., Moser C.C., and Dutton P.L. Design and engineering of photosynthetic light-harvesting and electron transfer using length, time, and energy scales. Biochim. Biophys. Acta 1757 (2006) 90-105
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 90-105
    • Noy, D.1    Moser, C.C.2    Dutton, P.L.3
  • 13
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page C.C., Moser C.C., and Dutton P.L. Mechanism for electron transfer within and between proteins. Curr. Opin. Chem. Biol. 7 (2003) 551-556
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 14
    • 36849037465 scopus 로고    scopus 로고
    • Engineering model proteins for Photosystem II function
    • Wydrzynski T., Hillier W., and Conlan B. Engineering model proteins for Photosystem II function. Photosyn. Res. 94 (2007) 225-233
    • (2007) Photosyn. Res. , vol.94 , pp. 225-233
    • Wydrzynski, T.1    Hillier, W.2    Conlan, B.3
  • 16
    • 18844438921 scopus 로고    scopus 로고
    • Design of a redox-linked active metal site: manganese bound to bacterial reaction centers at a site resembling that of Photosystem II
    • Thielges M., Uyeda G., Camara-Artigas A., Kalman L., Williams J.C., and Allen J.P. Design of a redox-linked active metal site: manganese bound to bacterial reaction centers at a site resembling that of Photosystem II. Biochemistry 44 (2005) 7389-7394
    • (2005) Biochemistry , vol.44 , pp. 7389-7394
    • Thielges, M.1    Uyeda, G.2    Camara-Artigas, A.3    Kalman, L.4    Williams, J.C.5    Allen, J.P.6
  • 17
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • Gray H.B., and Winkler J.R. Electron tunneling through proteins. Q. Rev. Biophys. 36 (2003) 341-372
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 19
    • 0027405142 scopus 로고
    • Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C-terminally extended variant
    • Andrews S.C., Smith J.M.A., Hawkins C., Williams J.M., Harrison P.M., and Guest J.R. Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C-terminally extended variant. Eur. J. Biochem. 213 (1993) 329-338
    • (1993) Eur. J. Biochem. , vol.213 , pp. 329-338
    • Andrews, S.C.1    Smith, J.M.A.2    Hawkins, C.3    Williams, J.M.4    Harrison, P.M.5    Guest, J.R.6
  • 20
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis G.D., Elisee C., Newham D.M., and Harrison R.G. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 65 (1999) 382-388
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 21
    • 0028467772 scopus 로고
    • Structure of a unique twofold symmetrical heme-binding site
    • Frolow F., Kalb A.J., and Yariv J. Structure of a unique twofold symmetrical heme-binding site. Nat. Struct. Biol. 1 (1994) 453-460
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 24
    • 0030608152 scopus 로고    scopus 로고
    • Ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., and Arosio P. Ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275 (1996) 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 25
    • 0025752671 scopus 로고
    • Bacterial 4-alpha-helical bundle cytochromes
    • Moore G.R. Bacterial 4-alpha-helical bundle cytochromes. Biochim. Biophys. Acta 1058 (1991) 38-41
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 38-41
    • Moore, G.R.1
  • 26
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methylethylketone
    • Teale F.W.J. Cleavage of the haem-protein link by acid methylethylketone. Biochim. Biophys. Acta 35 (1959) 543
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 28
    • 0033628213 scopus 로고    scopus 로고
    • Chapter 16: Manganese Catalases
    • Sigel H.S., and A. (Eds), Marcell Dekker, Inc., New York
    • Yoder D.W., Hwang J., and Penner-Hahn J.E. Chapter 16: Manganese Catalases. In: Sigel H.S., and A. (Eds). Manganese and Its Role in Biological Processes vol. 37 (2000), Marcell Dekker, Inc., New York 527-557
    • (2000) Manganese and Its Role in Biological Processes , vol.37 , pp. 527-557
    • Yoder, D.W.1    Hwang, J.2    Penner-Hahn, J.E.3
  • 31
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of Photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of Photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 33
    • 0037417760 scopus 로고    scopus 로고
    • Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation
    • Razeghifard A.R., and Wydrzynski T. Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation. Biochemistry 42 (2003) 1024-1030
    • (2003) Biochemistry , vol.42 , pp. 1024-1030
    • Razeghifard, A.R.1    Wydrzynski, T.2
  • 34
    • 0002207090 scopus 로고
    • Electron-paramagnetic-res spectra of quintet ferrous myoglobin and a model heme compound
    • Hendrich M.P., and Debrunner P.G. Electron-paramagnetic-res spectra of quintet ferrous myoglobin and a model heme compound. J. Magn. Reson. 78 (1988) 133-141
    • (1988) J. Magn. Reson. , vol.78 , pp. 133-141
    • Hendrich, M.P.1    Debrunner, P.G.2
  • 35
    • 0024728608 scopus 로고
    • Integer-spin electron-paramagnetic resonance of iron proteins
    • Hendrich M.P., and Debrunner P.G. Integer-spin electron-paramagnetic resonance of iron proteins. Biophys. J. 56 (1989) 489-506
    • (1989) Biophys. J. , vol.56 , pp. 489-506
    • Hendrich, M.P.1    Debrunner, P.G.2
  • 38
    • 0345074091 scopus 로고    scopus 로고
    • Outer sphere mutagenesis of Lactobacillus plantarum manganese catalase disrupts the cluster core - mechanistic implications
    • Whittaker M.M., Barynin V.V., Igarashi T., and Whittaker J.W. Outer sphere mutagenesis of Lactobacillus plantarum manganese catalase disrupts the cluster core - mechanistic implications. Eur. J. Biochem. 270 (2003) 1102-1116
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1102-1116
    • Whittaker, M.M.1    Barynin, V.V.2    Igarashi, T.3    Whittaker, J.W.4
  • 39
    • 0034685473 scopus 로고    scopus 로고
    • Dual-mode EPR detects the initial intermediate in photoassembly of the Photosystem II Mn cluster: the influence of amino acid residue 170 of the D1 polypeptide on Mn coordination
    • Campbell K.A., Force D.A., Nixon P.J., Dole F., Diner B.A., and Britt R.D. Dual-mode EPR detects the initial intermediate in photoassembly of the Photosystem II Mn cluster: the influence of amino acid residue 170 of the D1 polypeptide on Mn coordination. J. Am. Chem. Soc. 122 (2000) 3754-3761
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3754-3761
    • Campbell, K.A.1    Force, D.A.2    Nixon, P.J.3    Dole, F.4    Diner, B.A.5    Britt, R.D.6
  • 40
  • 41
    • 0034709839 scopus 로고    scopus 로고
    • An electron paramagnetic resonance study of Mn2(H2O)(OAc)4(tmeda)2 (tmeda = N,N,N′,N′-Tetramethylethylenediamine): a model for dinuclear manganese enzyme active sites
    • Howard T., Telser J., and DeRose V.J. An electron paramagnetic resonance study of Mn2(H2O)(OAc)4(tmeda)2 (tmeda = N,N,N′,N′-Tetramethylethylenediamine): a model for dinuclear manganese enzyme active sites. Inorg. Chem. 39 (2000) 3379-3385
    • (2000) Inorg. Chem. , vol.39 , pp. 3379-3385
    • Howard, T.1    Telser, J.2    DeRose, V.J.3
  • 42
    • 0025227911 scopus 로고
    • ESR spectroscopy of the binuclear cluster of manganese ions in the active center of Mn-catalase from Thermus thermophilus
    • Khangulov S.V., Barynin V.V., Voevodskaya N.V., and Grebenko A.I. ESR spectroscopy of the binuclear cluster of manganese ions in the active center of Mn-catalase from Thermus thermophilus. Biochim. Biophys. Acta 1020 (1990) 305-310
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 305-310
    • Khangulov, S.V.1    Barynin, V.V.2    Voevodskaya, N.V.3    Grebenko, A.I.4
  • 43
    • 0027948056 scopus 로고
    • Structural and functional models of the dimanganese catalase enzymes. 2. Structure, electrochemical, redox, and EPR properties
    • Pessiki P.J., Khangulov S.V., Ho D.M., and Dismukes G.C. Structural and functional models of the dimanganese catalase enzymes. 2. Structure, electrochemical, redox, and EPR properties. J. Am. Chem. Soc. 116 (1994) 891-897
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 891-897
    • Pessiki, P.J.1    Khangulov, S.V.2    Ho, D.M.3    Dismukes, G.C.4
  • 44
    • 20444472906 scopus 로고    scopus 로고
    • Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus
    • Epel B., Schafer K.O., Quentmeier A., Friedrich C., and Lubitz W. Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus. J. Biol. Inorg. Chem. 10 (2005) 636-642
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 636-642
    • Epel, B.1    Schafer, K.O.2    Quentmeier, A.3    Friedrich, C.4    Lubitz, W.5
  • 45
    • 0000063535 scopus 로고    scopus 로고
    • Manganese enzymes with binuclear active sites
    • Dismukes G.C. Manganese enzymes with binuclear active sites. Chem. Rev. 96 (1996) 2909-2926
    • (1996) Chem. Rev. , vol.96 , pp. 2909-2926
    • Dismukes, G.C.1
  • 46
    • 0142075315 scopus 로고    scopus 로고
    • Quantitative analysis of dinuclear manganese(II) EPR spectra
    • Golombek A.P., and Hendrich M.P. Quantitative analysis of dinuclear manganese(II) EPR spectra. J. Magn. Reson. 165 (2003) 33-48
    • (2003) J. Magn. Reson. , vol.165 , pp. 33-48
    • Golombek, A.P.1    Hendrich, M.P.2
  • 47
    • 34249875410 scopus 로고    scopus 로고
    • Characterization of the catalytically active Mn(II)-loaded argE-encoded N-acetyl-l-ornithine deacetylase from Escherichia coli
    • McGregor W.C., Swierczek S.I., Bennett B., and Holz R.C. Characterization of the catalytically active Mn(II)-loaded argE-encoded N-acetyl-l-ornithine deacetylase from Escherichia coli. J. Biol. Inorg. Chem. 12 (2007) 603-613
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 603-613
    • McGregor, W.C.1    Swierczek, S.I.2    Bennett, B.3    Holz, R.C.4
  • 48
    • 31044441352 scopus 로고    scopus 로고
    • Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis
    • Schaab M.R., Barney B.M., and Francisco W.A. Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis. Biochemistry 45 (2006) 1009-1016
    • (2006) Biochemistry , vol.45 , pp. 1009-1016
    • Schaab, M.R.1    Barney, B.M.2    Francisco, W.A.3
  • 49
    • 0030066104 scopus 로고    scopus 로고
    • Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Archrobacter globiformis CM-2
    • Whiting A.K., Boldt Y.R., Hendrich M.P., Wackett L.P., and Que L. Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Archrobacter globiformis CM-2. Biochemistry 35 (1996) 160-170
    • (1996) Biochemistry , vol.35 , pp. 160-170
    • Whiting, A.K.1    Boldt, Y.R.2    Hendrich, M.P.3    Wackett, L.P.4    Que, L.5
  • 50
    • 1542274450 scopus 로고    scopus 로고
    • Structural, spectroscopic, and reactivity models for the manganese catalases
    • Wu A.J., Penner-Hahn J.E., and Pecoraro V.L. Structural, spectroscopic, and reactivity models for the manganese catalases. Chem. Rev. 104 (2004) 903-938
    • (2004) Chem. Rev. , vol.104 , pp. 903-938
    • Wu, A.J.1    Penner-Hahn, J.E.2    Pecoraro, V.L.3
  • 51
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang X., Le Brun N.E., Thomson A.J., Moore G.R., and Chasteen N.D. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry 39 (2000) 4915-4923
    • (2000) Biochemistry , vol.39 , pp. 4915-4923
    • Yang, X.1    Le Brun, N.E.2    Thomson, A.J.3    Moore, G.R.4    Chasteen, N.D.5
  • 54
    • 33947396788 scopus 로고    scopus 로고
    • Characterization of the tyrosine-Z radical and its environment in the spin-coupled S(2)Tyr(Z)(center dot) state of Photosystem II from Thermosynechococcus elongatus
    • Un S., Boussac A., and Sugiura M. Characterization of the tyrosine-Z radical and its environment in the spin-coupled S(2)Tyr(Z)(center dot) state of Photosystem II from Thermosynechococcus elongatus. Biochemistry 46 (2007) 3138-3150
    • (2007) Biochemistry , vol.46 , pp. 3138-3150
    • Un, S.1    Boussac, A.2    Sugiura, M.3
  • 56
    • 0030592840 scopus 로고    scopus 로고
    • Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites
    • LeBrun N.E., Keech A.M., Mauk M.R., Mauk A.G., Andrews S.C., Thomson A.J., and Moore G.R. Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. FEBS Lett. 397 (1996) 159-163
    • (1996) FEBS Lett. , vol.397 , pp. 159-163
    • LeBrun, N.E.1    Keech, A.M.2    Mauk, M.R.3    Mauk, A.G.4    Andrews, S.C.5    Thomson, A.J.6    Moore, G.R.7
  • 57
    • 0037951337 scopus 로고    scopus 로고
    • Defining metal ion inhibitor interactions with recombinant human H- and L-chain ferritins and site-directed variants: an isothermal titration calorimetry study
    • Bou-Abdallah F., Arosio P., Levi S., Janus-Chandler C., and Chasteen N.D. Defining metal ion inhibitor interactions with recombinant human H- and L-chain ferritins and site-directed variants: an isothermal titration calorimetry study. J. Biol. Inorg. Chem. 8 (2003) 489-497
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 489-497
    • Bou-Abdallah, F.1    Arosio, P.2    Levi, S.3    Janus-Chandler, C.4    Chasteen, N.D.5
  • 58
    • 38049100652 scopus 로고    scopus 로고
    • Photoassembly of the water-oxidizing complex in Photosystem II
    • Dasgupta J., Ananyev G.M., and Dismukes G.C. Photoassembly of the water-oxidizing complex in Photosystem II. Coord. Chem. Rev. 252 (2008) 347-360
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 347-360
    • Dasgupta, J.1    Ananyev, G.M.2    Dismukes, G.C.3
  • 59
    • 0036026550 scopus 로고    scopus 로고
    • Studies of copper(II)-binding to bacterioferritin and its effect on iron(II) oxidation
    • Baaghil S., Thomson A.J., Moore G.R., and Le Brun N.E. Studies of copper(II)-binding to bacterioferritin and its effect on iron(II) oxidation. J. Chem. Soc. Dalton (2002) 811-818
    • (2002) J. Chem. Soc. Dalton , pp. 811-818
    • Baaghil, S.1    Thomson, A.J.2    Moore, G.R.3    Le Brun, N.E.4
  • 61
    • 4344712784 scopus 로고    scopus 로고
    • 2.6 Angstrom resolution crystal structure of the bacterioferritin from Azotobacter vinelandii
    • Liu H.L., Zhou H.N., Xing W.M., Zhao H.F., Li S.X., Huang J.F., and Bi R.C. 2.6 Angstrom resolution crystal structure of the bacterioferritin from Azotobacter vinelandii. FEBS Lett. 573 (2004) 93-98
    • (2004) FEBS Lett. , vol.573 , pp. 93-98
    • Liu, H.L.1    Zhou, H.N.2    Xing, W.M.3    Zhao, H.F.4    Li, S.X.5    Huang, J.F.6    Bi, R.C.7
  • 62
    • 0344412956 scopus 로고    scopus 로고
    • Core formation in Escherichia coli bacterioferritin requires a functional
    • Baaghil S., Lewin A., Moore G.R., and Le Brun N.E. Core formation in Escherichia coli bacterioferritin requires a functional. Biochemistry 42 (2003) 14047-14056
    • (2003) Biochemistry , vol.42 , pp. 14047-14056
    • Baaghil, S.1    Lewin, A.2    Moore, G.R.3    Le Brun, N.E.4
  • 63
    • 0030043242 scopus 로고    scopus 로고
    • Investigation of the differences in the local protein environments surrounding tyrosine radicals Y-Z(center dot) and Y-D(center dot) in Photosystem II using wild-type and the D2-Tyr160Phe mutant of Synechocystis 6803
    • Tang X.S., Zheng M., Chisholm D.A., Dismukes G.C., and Diner B.A. Investigation of the differences in the local protein environments surrounding tyrosine radicals Y-Z(center dot) and Y-D(center dot) in Photosystem II using wild-type and the D2-Tyr160Phe mutant of Synechocystis 6803. Biochemistry 35 (1996) 1475-1484
    • (1996) Biochemistry , vol.35 , pp. 1475-1484
    • Tang, X.S.1    Zheng, M.2    Chisholm, D.A.3    Dismukes, G.C.4    Diner, B.A.5
  • 64
    • 33144465946 scopus 로고    scopus 로고
    • Charge separation kinetics in intact Photosystem II core particles is trap-limited. A picosecond fluorescence study
    • Miloslavina Y., Szczepaniak M., Muller M.G., Sander J., Nowaczyk M., Rogner M., and Holzwarth A.R. Charge separation kinetics in intact Photosystem II core particles is trap-limited. A picosecond fluorescence study. Biochemistry 45 (2006) 2436-2442
    • (2006) Biochemistry , vol.45 , pp. 2436-2442
    • Miloslavina, Y.1    Szczepaniak, M.2    Muller, M.G.3    Sander, J.4    Nowaczyk, M.5    Rogner, M.6    Holzwarth, A.R.7
  • 65
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo M.A. Ferritins, iron uptake and storage from the bacterioferritin viewpoint. EMBO J. 22 (2003) 1959-1968
    • (2003) EMBO J. , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 66
    • 43149108146 scopus 로고    scopus 로고
    • Reactivity of an aminopyridine [LMnII](2+) complex with H2O2. Detection of intermediates at low temperature
    • Groni S., Dorlet P., Blain G., Bourcier S., Guillot R., and Anxolabehere-Mallart E. Reactivity of an aminopyridine [LMnII](2+) complex with H2O2. Detection of intermediates at low temperature. Inorg. Chem. 47 (2008) 3166-3172
    • (2008) Inorg. Chem. , vol.47 , pp. 3166-3172
    • Groni, S.1    Dorlet, P.2    Blain, G.3    Bourcier, S.4    Guillot, R.5    Anxolabehere-Mallart, E.6
  • 67
    • 19944408376 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the cobalt and manganese oxyhydroxide cores formed in horse spleen ferritin
    • Zhang B., Harb J.N., Davis R.C., Kim J.W., Chu S.H., Choi S., Miller T., and Watt G.D. Kinetic and thermodynamic characterization of the cobalt and manganese oxyhydroxide cores formed in horse spleen ferritin. Inorg. Chem. 44 (2005) 3738-3745
    • (2005) Inorg. Chem. , vol.44 , pp. 3738-3745
    • Zhang, B.1    Harb, J.N.2    Davis, R.C.3    Kim, J.W.4    Chu, S.H.5    Choi, S.6    Miller, T.7    Watt, G.D.8
  • 73
    • 0001127922 scopus 로고
    • Active-site spectral studies on manganese superoxide-dismutase
    • Whittaker J.W., and Whittaker M.M. Active-site spectral studies on manganese superoxide-dismutase. J. Am. Chem. Soc. 113 (1991) 5528-5540
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5528-5540
    • Whittaker, J.W.1    Whittaker, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.