메뉴 건너뛰기




Volumn 45, Issue 20, 2006, Pages 8372-8381

Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; METHANE MONOOXYGENASE; OXYGENASE;

EID: 33750371559     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic060739v     Document Type: Article
Times cited : (79)

References (40)
  • 2
    • 4444257275 scopus 로고    scopus 로고
    • Biological methane oxidation: Regulation, biochemistry, and active site structure of particulate methane monooxygenase
    • Lieberman, R. L.; Rosenzweig, A. C. Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 2004, 39, 147-164.
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 147-164
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 3
    • 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. 2001, 40, 2782-2807.
    • (2001) Angew. Chem., Int. Ed. , 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
  • 4
    • 0036038187 scopus 로고    scopus 로고
    • Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea
    • Arp, D. J.; Sayavedra-Soto, L. A.; Hommes, N. G. Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 2002, 178, 250-255.
    • (2002) Arch. Microbiol. , vol.178 , pp. 250-255
    • Arp, D.J.1    Sayavedra-Soto, L.A.2    Hommes, N.G.3
  • 5
    • 0020559210 scopus 로고
    • Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane oxidizing organisms: Studies in batch and continuous cultures
    • Stanley, S. H.; Prior, S. D.; Leak, D. J.; Dalton, H. Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane oxidizing organisms: studies in batch and continuous cultures. Biotechnol. Lett. 1983, 5, 487-492.
    • (1983) Biotechnol. Lett. , vol.5 , pp. 487-492
    • Stanley, S.H.1    Prior, S.D.2    Leak, D.J.3    Dalton, H.4
  • 6
    • 0021911405 scopus 로고
    • The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath)
    • Prior, S. D.; Dalton, H. The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 1985, 131, 155-163.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 155-163
    • Prior, S.D.1    Dalton, H.2
  • 7
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig, A. C.; Frederick, C. A.; Lippard, S. J.; Nordlund, P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 1993, 366, 537-543.
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.C.1    Frederick, C.A.2    Lippard, S.J.3    Nordlund, P.4
  • 8
    • 19744365629 scopus 로고    scopus 로고
    • Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers
    • Beauvais, L. G.; Lippard, S. J. Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers. J. Am. Chem. Soc. 2005, 127, 7370-7378.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7370-7378
    • Beauvais, L.G.1    Lippard, S.J.2
  • 9
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
    • Lieberman, R. L.; Rosenzweig, A. C. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 2005, 434, 177-182.
    • (2005) Nature , vol.434 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 10
    • 0037386563 scopus 로고    scopus 로고
    • Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
    • Lieberman, R. L.; Shrestha, D. B.; Doan, P. E.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3820-3825.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3820-3825
    • Lieberman, R.L.1    Shrestha, D.B.2    Doan, P.E.3    Hoffman, B.M.4    Stemmler, T.L.5    Rosenzweig, A.C.6
  • 12
    • 0348087046 scopus 로고    scopus 로고
    • The membrane-associated form of methane monooxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
    • Basu, P.; Katterle, B.; Andersson, K. K.; Dalton, H. The membrane-associated form of methane monooxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 2003, 369, 417-427.
    • (2003) Biochem. J. , vol.369 , pp. 417-427
    • Basu, P.1    Katterle, B.2    Andersson, K.K.3    Dalton, H.4
  • 13
    • 0037037518 scopus 로고    scopus 로고
    • Synthesis and characterization of completely delocalized mixed-valent dicopper complexes
    • Gupta, R.; Zhang, Z. H.; Powell, D.; Hendrich, M. P.; Borovik, A. S. Synthesis and characterization of completely delocalized mixed-valent dicopper complexes. Inorg. Chem. 2002, 41, 5100-5106.
    • (2002) Inorg. Chem. , vol.41 , pp. 5100-5106
    • Gupta, R.1    Zhang, Z.H.2    Powell, D.3    Hendrich, M.P.4    Borovik, A.S.5
  • 14
    • 0001090154 scopus 로고    scopus 로고
    • Mixed-Valence Cu(I)-Cu(II) and Heterodimetallic Cu(I)-M(II) Bis(carboxylate-bridged) Complexes: Structural, Electrochemical, and Spectroscopic Investigations
    • LeCloux, D. D.; Davydov, R.; Lippard, S. J. Mixed-Valence Cu(I)-Cu(II) and Heterodimetallic Cu(I)-M(II) Bis(carboxylate-bridged) Complexes: Structural, Electrochemical, and Spectroscopic Investigations. Inorg Chem 1998, 37 (26), 6814-6826.
    • (1998) Inorg Chem , vol.37 , Issue.26 , pp. 6814-6826
    • LeCloux, D.D.1    Davydov, R.2    Lippard, S.J.3
  • 16
    • 0642303383 scopus 로고    scopus 로고
    • Relativistic calculations of spin-dependent X-ray absorption spectra
    • Ankudinov, A. L.; Rehr, J. J. Relativistic calculations of spin-dependent X-ray absorption spectra. Phys. Rev. B 1997, 56, R1712-R1715.
    • (1997) Phys. Rev. B , vol.56
    • Ankudinov, A.L.1    Rehr, J.J.2
  • 17
    • 35949022427 scopus 로고
    • Extended X-ray absorption fine structure - Its strengths and limitations as a structural tool
    • Lee, P. A.; Citrin, P. H.; Eisenberger, P.; Kincaid, B. M. Extended X-ray absorption fine structure - its strengths and limitations as a structural tool. Rev. Mod. Phys. 1981, 53 (4), 769-806.
    • (1981) Rev. Mod. Phys. , vol.53 , Issue.4 , pp. 769-806
    • Lee, P.A.1    Citrin, P.H.2    Eisenberger, P.3    Kincaid, B.M.4
  • 20
    • 0032506972 scopus 로고    scopus 로고
    • EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor
    • Riggs-Gelasco, P. J.; Shu, L.; Chen, S.; Burdi, D.; Huynh, B. H.; Que, L., Jr.; Stubbe, J. EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor. J. Am. Chem. Soc. 1998, 120, 849-860.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 849-860
    • Riggs-Gelasco, P.J.1    Shu, L.2    Chen, S.3    Burdi, D.4    Huynh, B.H.5    Que Jr., L.6    Stubbe, J.7
  • 23
    • 33845283452 scopus 로고
    • X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen
    • Kau, L.-S.; Spira-Solomon, D. J.; Penner-Hahn, J. E.; Hodgson, K. O.; Solomon, E. I. X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen. J. Am. Chem. Soc. 1987, 109, 6433-6442.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-6442
    • Kau, L.-S.1    Spira-Solomon, D.J.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 24
    • 0029645280 scopus 로고
    • Structure of CuB in the binuclear heme-copper center of the cytochrome aa3-type quinol oxidase from Bacillus subtilis: An ENDOR and EXAFS study
    • Fann, Y. C.; Ahmed, I.; Blackburn, N. J.; Boswell, J. S.; Verkhovskaya, M. L.; Hoffman, B. M.; Wikstrom, M. Structure of CuB in the binuclear heme-copper center of the cytochrome aa3-type quinol oxidase from Bacillus subtilis: an ENDOR and EXAFS study. Biochemistry 1995, 34 (32), 10245-10255.
    • (1995) Biochemistry , vol.34 , Issue.32 , pp. 10245-10255
    • Fann, Y.C.1    Ahmed, I.2    Blackburn, N.J.3    Boswell, J.S.4    Verkhovskaya, M.L.5    Hoffman, B.M.6    Wikstrom, M.7
  • 27
    • 0000276546 scopus 로고
    • An EXAFS calculation using known four-body correlations
    • Loeffen, P. W.; Pettifer, R. F. An EXAFS calculation using known four-body correlations. Phys. Rev. Lett. 1995, 76 (4), 636-639.
    • (1995) Phys. Rev. Lett. , vol.76 , Issue.4 , pp. 636-639
    • Loeffen, P.W.1    Pettifer, R.F.2
  • 28
    • 0030857696 scopus 로고    scopus 로고
    • EXAFS comparison of the dimanganese core structures of manganese catalase, arginase and manganese-substituted ribonucleotide reductase and hemerythrin
    • Stemmler, T. L.; Sossong, T. M., Jr.; Goldstein, J. I.; Ash, D. E.; Elgren, T. E.; Kurtz, D. M., Jr.; Penner-Hahn, J. E. EXAFS comparison of the dimanganese core structures of manganese catalase, arginase and manganese-substituted ribonucleotide reductase and hemerythrin. Biochemistry 1997, 36 (32), 9847-9858.
    • (1997) Biochemistry , vol.36 , Issue.32 , pp. 9847-9858
    • Stemmler, T.L.1    Sossong Jr., T.M.2    Goldstein, J.I.3    Ash, D.E.4    Elgren, T.E.5    Kurtz Jr., D.M.6    Penner-Hahn, J.E.7
  • 29
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez, S. E.; Huang, D.; Szczepaniak, A.; Cramer, W. A.; Smith, J. L. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 1994, 2 (2), 95-105.
    • (1994) Structure , vol.2 , Issue.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 30
    • 0345586061 scopus 로고    scopus 로고
    • Structural and functional models for the dinuclear copper active site in catechol oxidases: Syntheses, X-ray crystal structures, magnetic and spectral Properties, and X-ray absorption spectroscopic studies in solid state and in solution
    • Zippel, F.; Ahlers, F.; Werner, R.; Haase, W.; Nolting, H. F.; Krebs, B. Structural and functional models for the dinuclear copper active site in catechol oxidases: syntheses, X-ray crystal structures, magnetic and spectral Properties, and X-ray absorption spectroscopic studies in solid state and in solution. Inorg. Chem. 1996, 35 (11), 3409-3419.
    • (1996) Inorg. Chem. , vol.35 , Issue.11 , pp. 3409-3419
    • Zippel, F.1    Ahlers, F.2    Werner, R.3    Haase, W.4    Nolting, H.F.5    Krebs, B.6
  • 32
    • 0033153281 scopus 로고    scopus 로고
    • Selenomethionine-substituted Thermus thermophilus cytochrome ba3: Characterization of the CUA site by Se and Cu K-EXAFS
    • Blackburn, N. J.; Ralle, M.; Gomez, E.; Hill, M. G.; Pastuszyn, A.; Sanders, D.; Fee, J. A. Selenomethionine-substituted Thermus thermophilus cytochrome ba3: characterization of the CUA site by Se and Cu K-EXAFS. Biochemistry 1999, 38 (22), 7075-7084.
    • (1999) Biochemistry , vol.38 , Issue.22 , pp. 7075-7084
    • Blackburn, N.J.1    Ralle, M.2    Gomez, E.3    Hill, M.G.4    Pastuszyn, A.5    Sanders, D.6    Fee, J.A.7
  • 35
    • 0030802191 scopus 로고    scopus 로고
    • X-ray absorption studies on the mixed-valence and fully reduced forms of the soluble CUA domains of cytochrome c oxidase
    • Blackburn, N. J.; de Vries, S.; Barr, M. E.; Houser, R. P.; Tolman, W. B.; Sanders, D.; Fee, J. A. X-ray absorption studies on the mixed-valence and fully reduced forms of the soluble CUA domains of cytochrome c oxidase. J. Am. Chem. Soc. 1997, 119, 6135-6143.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6135-6143
    • Blackburn, N.J.1    De Vries, S.2    Barr, M.E.3    Houser, R.P.4    Tolman, W.B.5    Sanders, D.6    Fee, J.A.7
  • 36
  • 37
    • 77957027443 scopus 로고
    • Mixed valence chemistry - A survey and classification
    • Robin, M. B.; Day, P. Mixed valence chemistry - a survey and classification. Adv. Inorg. Chem. Radiochem. 1967, 10, 247-423.
    • (1967) Adv. Inorg. Chem. Radiochem. , vol.10 , pp. 247-423
    • Robin, M.B.1    Day, P.2
  • 38
    • 0030982183 scopus 로고    scopus 로고
    • Copper a of cytochrome c oxidase, a novel, long-embattled biological electron-transfer site
    • Beinert, H. Copper A of cytochrome c oxidase, a novel, long-embattled biological electron-transfer site. Eur. J. Biochem. 1997, 245, 521-532.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 521-532
    • Beinert, H.1
  • 39
    • 4444276791 scopus 로고    scopus 로고
    • pH-dependent transition between delocalized and trapped valence states of a CUA center and its possible role in proton-coupled electron transfer
    • Hwang, H. J.; Lu, Y. pH-dependent transition between delocalized and trapped valence states of a CUA center and its possible role in proton-coupled electron transfer. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 12842-12847.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12842-12847
    • Hwang, H.J.1    Lu, Y.2
  • 40
    • 33845182877 scopus 로고
    • Detailed spectroscopic analysis of half-met hemocyanins: Mixed-valent contributions to electronic properties and structure
    • Westmoreland, T. D.; Wilcox, D. E.; Baldwin, M. J.; Mims, W. B.; Solomon, E. I. Detailed spectroscopic analysis of half-met hemocyanins: mixed-valent contributions to electronic properties and structure. J. Am. Chem. Soc. 1989, 111, 6106-6123.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6106-6123
    • Westmoreland, T.D.1    Wilcox, D.E.2    Baldwin, M.J.3    Mims, W.B.4    Solomon, E.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.