-
3
-
-
15044356424
-
Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
-
Lieberman, R.L. and Rosenzweig, A.C. (2005) Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434, 177-182
-
(2005)
Nature
, vol.434
, pp. 177-182
-
-
Lieberman, R.L.1
Rosenzweig, A.C.2
-
4
-
-
23944513777
-
Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)
-
Kitmitto, A., Myronova, N., Basu, P. and Dalton, H. (2005) Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 44, 10954-10965
-
(2005)
Biochemistry
, vol.44
, pp. 10954-10965
-
-
Kitmitto, A.1
Myronova, N.2
Basu, P.3
Dalton, H.4
-
5
-
-
0034192166
-
Regulation of expression of methane monooxygenases by copper ions
-
Murrell, J.C., McDonald, I.R. and Gilbert, B. (2000) Regulation of expression of methane monooxygenases by copper ions. Trends Microbiol. 8, 221-225
-
(2000)
Trends Microbiol
, vol.8
, pp. 221-225
-
-
Murrell, J.C.1
McDonald, I.R.2
Gilbert, B.3
-
6
-
-
34547768909
-
Substrate trafficking and dioxygen activation in bacterial multicomponent monooxygenases
-
Murray, L.J. and Lippard, S.J. (2007) Substrate trafficking and dioxygen activation in bacterial multicomponent monooxygenases. Acc. Chem. Res. 40, 466-474
-
(2007)
Acc. Chem. Res
, vol.40
, pp. 466-474
-
-
Murray, L.J.1
Lippard, S.J.2
-
7
-
-
34547752024
-
Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase
-
Balasubramanian, R. and Rosenzweig, A.C. (2007) Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 40, 573-580
-
(2007)
Acc. Chem. Res
, vol.40
, pp. 573-580
-
-
Balasubramanian, R.1
Rosenzweig, A.C.2
-
8
-
-
4644230771
-
Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria
-
Chan, S.I., Chen, K.H.-C., Yu, S.S.-F., Chen, C.-L. and Kuo, S.S.-J. (2004) Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Biochemistry 43, 4421-4430
-
(2004)
Biochemistry
, vol.43
, pp. 4421-4430
-
-
Chan, S.I.1
Chen, K.H.-C.2
Yu, S.S.-F.3
Chen, C.-L.4
Kuo, S.S.-J.5
-
9
-
-
4444257275
-
Biological methane oxidation: Regulation, biochemistry, and active site structure of particulate methane monooxygenase
-
Lieberman, R.L. and Rosenzweig, A.C. (2004) Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 39, 147-164
-
(2004)
Crit. Rev. Biochem. Mol. Biol
, vol.39
, pp. 147-164
-
-
Lieberman, R.L.1
Rosenzweig, A.C.2
-
10
-
-
0032478599
-
The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme: Isolation and characterization
-
Nguyen, H.H., Elliott, S.J., Yip, J.H. and Chan, S.I. (1998) The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme: isolation and characterization. J. Biol. Chem. 273, 7957-7966
-
(1998)
J. Biol. Chem
, vol.273
, pp. 7957-7966
-
-
Nguyen, H.H.1
Elliott, S.J.2
Yip, J.H.3
Chan, S.I.4
-
11
-
-
0141960385
-
Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (Bath) with a hollow-fiber membrane bioreactor
-
Yu, S.S.-F., Chen, K.H.-C., Tseng, M.Y.-H., Wang, Y.-S., Tseng, C.-F., Chen, Y.-J., Huang, D.S. and Chan, S.I. (2003) Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (Bath) with a hollow-fiber membrane bioreactor. J. Bacteriol. 185, 5915-5924
-
(2003)
J. Bacteriol
, vol.185
, pp. 5915-5924
-
-
Yu, S.S.-F.1
Chen, K.H.-C.2
Tseng, M.Y.-H.3
Wang, Y.-S.4
Tseng, C.-F.5
Chen, Y.-J.6
Huang, D.S.7
Chan, S.I.8
-
12
-
-
0141838951
-
The membrane-associated methane monooxygenase pMMO and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus Bath
-
Choi, D.W., Kunz, R.C., Boyd, E.S., Semrau, J.D., Antholine, W.E., Han, J.I., Zahn, J.A., Boyd, J.M., de la Mora, A.M. and DiSpirito, A.A. (2003) The membrane-associated methane monooxygenase pMMO and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus Bath. J. Bacteriol. 185, 5755-5764
-
(2003)
J. Bacteriol
, vol.185
, pp. 5755-5764
-
-
Choi, D.W.1
Kunz, R.C.2
Boyd, E.S.3
Semrau, J.D.4
Antholine, W.E.5
Han, J.I.6
Zahn, J.A.7
Boyd, J.M.8
de la Mora, A.M.9
DiSpirito, A.A.10
-
13
-
-
0037386563
-
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. and Rosenzweig, A.C. (2003) 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. 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
-
14
-
-
0348087046
-
The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
-
Basu, P., Katterle, B., Andersson, K.K. and Dalton, H. (2003) The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369, 417-427
-
(2003)
Biochem. J
, vol.369
, pp. 417-427
-
-
Basu, P.1
Katterle, B.2
Andersson, K.K.3
Dalton, H.4
-
15
-
-
27744443429
-
The catalytic copper clusters of the particulate methane monooxygenase from methanotropic bacteria: Electron paramagnetic resonance spectral simulations
-
Hung, S.-C., Chen, C.-L., Chen, K.H.-C., Yu, S.S.-F. and Chan, S.I. (2004) The catalytic copper clusters of the particulate methane monooxygenase from methanotropic bacteria: electron paramagnetic resonance spectral simulations. J. Chin. Chem. Soc. 51, 1229-1244
-
(2004)
J. Chin. Chem. Soc
, vol.51
, pp. 1229-1244
-
-
Hung, S.-C.1
Chen, C.-L.2
Chen, K.H.-C.3
Yu, S.S.-F.4
Chan, S.I.5
-
16
-
-
6344293042
-
The copper clusters in the particulate methane monooxygenase (pMMO) from Methylococcus capsulatus (Bath)
-
Chen, K.H.-C., Chen, C.-L., Tseng, C.-F., Yu, S.S.-F., Ke, S.-C., Lee, J.-F., Nguyen, H.T., Elliott, S.J., Alben, J.O. and Chan, S.I. (2004) The copper clusters in the particulate methane monooxygenase (pMMO) from Methylococcus capsulatus (Bath). J. Chin. Chem. Soc. 51, 1081-1098
-
(2004)
J. Chin. Chem. Soc
, vol.51
, pp. 1081-1098
-
-
Chen, K.H.-C.1
Chen, C.-L.2
Tseng, C.-F.3
Yu, S.S.-F.4
Ke, S.-C.5
Lee, J.-F.6
Nguyen, H.T.7
Elliott, S.J.8
Alben, J.O.9
Chan, S.I.10
-
17
-
-
12644275421
-
X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxgyenase from Methylococcus capsulatus (Bath): Cu(I) ions and their implications
-
Nguyen, H.-H.T., Nakagawa, K.H., Hedman, B., Elliott, S.J., Lidstrom, M.E., Hodgson, K.O. and Chan, S.I. (1996) X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxgyenase from Methylococcus capsulatus (Bath): Cu(I) ions and their implications. J. Am. Chem. Soc. 118, 12766-12776
-
(1996)
J. Am. Chem. Soc
, vol.118
, pp. 12766-12776
-
-
Nguyen, H.-H.T.1
Nakagawa, K.H.2
Hedman, B.3
Elliott, S.J.4
Lidstrom, M.E.5
Hodgson, K.O.6
Chan, S.I.7
-
18
-
-
0028304991
-
The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
-
Nguyen, H.-H.T., Shiemke, A.K., Jacobs, S.J., Hales, B.J., Lidstrom, M.E. and Chan, S.I. (1994) The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269, 14995-15005
-
(1994)
J. Biol. Chem
, vol.269
, pp. 14995-15005
-
-
Nguyen, H.-H.T.1
Shiemke, A.K.2
Jacobs, S.J.3
Hales, B.J.4
Lidstrom, M.E.5
Chan, S.I.6
-
19
-
-
0030067648
-
Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
-
Zahn, J.A. and DiSpirito, A.A. (1996) Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 178, 1018-1029
-
(1996)
J. Bacteriol
, vol.178
, pp. 1018-1029
-
-
Zahn, J.A.1
DiSpirito, A.A.2
-
21
-
-
4644268662
-
Methanobactin, a copper-acquisition compound from methane oxidizing bacteria
-
Kim, H.J., Graham, D.W., DiSpirito, A.A., Alterman, M.A., Galeva, N., Larive, C.K., Asunskis, D. and Sherwood, P.M.A. (2004) Methanobactin, a copper-acquisition compound from methane oxidizing bacteria. Science 305, 1612-1615
-
(2004)
Science
, vol.305
, pp. 1612-1615
-
-
Kim, H.J.1
Graham, D.W.2
DiSpirito, A.A.3
Alterman, M.A.4
Galeva, N.5
Larive, C.K.6
Asunskis, D.7
Sherwood, P.M.A.8
-
23
-
-
0030987924
-
Low-frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium albus BG8
-
Yuan, H., Collins, M.L.P. and Antholine, W.E. (1997) Low-frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium albus BG8. J. Am. Chem. Soc. 119, 5073-5074
-
(1997)
J. Am. Chem. Soc
, vol.119
, pp. 5073-5074
-
-
Yuan, H.1
Collins, M.L.P.2
Antholine, W.E.3
-
25
-
-
0036566432
-
2+ sites of particulate methane mono-oxygenase of Methylococcus capsulatus (strain M) in membrane and pure dopamine β-mono-oxygenase of the adrenal medulla
-
2+ sites of particulate methane mono-oxygenase of Methylococcus capsulatus (strain M) in membrane and pure dopamine β-mono-oxygenase of the adrenal medulla. Biochem. J. 363, 677-686
-
(2002)
Biochem. J
, vol.363
, pp. 677-686
-
-
Katterle, B.1
Gvozdev, R.I.2
Abudu, N.3
Ljones, T.4
Andersson, K.K.5
-
26
-
-
0345355219
-
Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO
-
Yuan, H., Collins, M.L.P. and Antholine, W.E. (1998) Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO. J. Inorg. Biochem. 72, 179-185
-
(1998)
J. Inorg. Biochem
, vol.72
, pp. 179-185
-
-
Yuan, H.1
Collins, M.L.P.2
Antholine, W.E.3
-
27
-
-
33750371559
-
Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy
-
Lieberman, R.L., Kondapalli, K.C., Shrestha, D.B., Hakemian, A.S., Smith, S.M., Telser, J., Kuzelka, J., Gupta, R., Borovik, A.S., Lippard, S.J. et al. (2006) Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy. Inorg. Chem. 45, 8372-8381
-
(2006)
Inorg. Chem
, vol.45
, pp. 8372-8381
-
-
Lieberman, R.L.1
Kondapalli, K.C.2
Shrestha, D.B.3
Hakemian, A.S.4
Smith, S.M.5
Telser, J.6
Kuzelka, J.7
Gupta, R.8
Borovik, A.S.9
Lippard, S.J.10
-
28
-
-
27744520845
-
The quest for the particulate methane monooxygenase active site
-
Lieberman, R.L. and Rosenzweig, A.C. (2005) The quest for the particulate methane monooxygenase active site. Dalton Trans., 3390-3396
-
(2005)
Dalton Trans
, pp. 3390-3396
-
-
Lieberman, R.L.1
Rosenzweig, A.C.2
-
29
-
-
34247631187
-
Redox potentiometry studies of particulate methane monooxygenase: Support for a trinuclear copper cluster active site
-
Chan, S.I., Wang, V.C.C., Lai, J.C.H., Yu, S.S.F., Chen, P.P.Y., Chen, K.H.C., Chen, C.L. and Chan, M.K. (2007) Redox potentiometry studies of particulate methane monooxygenase: support for a trinuclear copper cluster active site. Angew. Chem. Int. Ed. 46, 1992-1994
-
(2007)
Angew. Chem. Int. Ed
, vol.46
, pp. 1992-1994
-
-
Chan, S.I.1
Wang, V.C.C.2
Lai, J.C.H.3
Yu, S.S.F.4
Chen, P.P.Y.5
Chen, K.H.C.6
Chen, C.L.7
Chan, M.K.8
-
30
-
-
36849049712
-
The C-terminal aqueous-exposed domain of the 45 kDa subunit of the particulate methane monooxygenase in Methylococcus capsulatus (Bath) is a Cu(I) sponge
-
Yu, S.S.F., Ji, C.Z., Wu, Y.P., Lee, T.L., Lai, C.H., Lin, S.C., Yang, Z.L., Wang, V.C.C., Chen, K.H.C. and Chan, S.I. (2007) The C-terminal aqueous-exposed domain of the 45 kDa subunit of the particulate methane monooxygenase in Methylococcus capsulatus (Bath) is a Cu(I) sponge. Biochemistry 46, 13762-13774
-
(2007)
Biochemistry
, vol.46
, pp. 13762-13774
-
-
Yu, S.S.F.1
Ji, C.Z.2
Wu, Y.P.3
Lee, T.L.4
Lai, C.H.5
Lin, S.C.6
Yang, Z.L.7
Wang, V.C.C.8
Chen, K.H.C.9
Chan, S.I.10
-
31
-
-
37549052557
-
Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus Bath: Evidence for a diiron center
-
Martinho, M., Choi, D.W., DiSpirito, A.A., Antholine, W.E., Semrau, J.D. and Münck, E. (2007) Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus Bath: evidence for a diiron center. J. Am. Chem. Soc. 129, 15783-15785
-
(2007)
J. Am. Chem. Soc
, vol.129
, pp. 15783-15785
-
-
Martinho, M.1
Choi, D.W.2
DiSpirito, A.A.3
Antholine, W.E.4
Semrau, J.D.5
Münck, E.6
-
32
-
-
0000139525
-
X-ray absorption, Mössbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase
-
DeWitt, J.G., Bentsen, J.G., Rosenzweig, A.C., Hedman, B., Green, J., Pilkington, S., Papaefthymiou, G.C., Dalton, H., Hodgson, K.O. and Lippard, S.J. (1991) X-ray absorption, Mössbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase. J. Am. Chem. Soc. 113, 9219-9235
-
(1991)
J. Am. Chem. Soc
, vol.113
, pp. 9219-9235
-
-
DeWitt, J.G.1
Bentsen, J.G.2
Rosenzweig, A.C.3
Hedman, B.4
Green, J.5
Pilkington, S.6
Papaefthymiou, G.C.7
Dalton, H.8
Hodgson, K.O.9
Lippard, S.J.10
-
33
-
-
0029379564
-
Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath)
-
Liu, K.E., Valentine, A.M., Wang, D., Huynh, B.H., Edmondson, D.E., Salifoglou, A. and Lippard, S.J. (1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J. Am. Chem. Soc. 117, 10174-10185
-
(1995)
J. Am. Chem. Soc
, vol.117
, pp. 10174-10185
-
-
Liu, K.E.1
Valentine, A.M.2
Wang, D.3
Huynh, B.H.4
Edmondson, D.E.5
Salifoglou, A.6
Lippard, S.J.7
-
34
-
-
18944380045
-
Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)
-
Karlsen, O.A., Ramsevik, L., Bruseth, L.J., Larsen, Ø., Brenner, A., Berven, F.S., Jensen, H.B. and Lillehaug, J.R. (2005) Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath). FEBS J. 272, 2428-2440
-
(2005)
FEBS J
, vol.272
, pp. 2428-2440
-
-
Karlsen, O.A.1
Ramsevik, L.2
Bruseth, L.J.3
Larsen, Ø.4
Brenner, A.5
Berven, F.S.6
Jensen, H.B.7
Lillehaug, J.R.8
-
35
-
-
46749114059
-
Isolation, purification, and characterization of hemerythrin from Methylococcus capsulatus (Bath)
-
Kao, W.-C., Wang, V.C.-C., Huang, Y.-C., Yu, S.S.-F., Chang, T.-C. and Chan, S.I. (2008) Isolation, purification, and characterization of hemerythrin from Methylococcus capsulatus (Bath). J. Inorg. Biochem. 102, 1607-1614
-
(2008)
J. Inorg. Biochem
, vol.102
, pp. 1607-1614
-
-
Kao, W.-C.1
Wang, V.C.-C.2
Huang, Y.-C.3
Yu, S.S.-F.4
Chang, T.-C.5
Chan, S.I.6
-
36
-
-
46049113886
-
The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b
-
Hakemian, A.S., Kondapalli, K.C., Telser, J., Hoffman, B.M., Stemmler, T.L. and Rosenzweig, A.C. (2008) The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry 47, 6793-6801
-
(2008)
Biochemistry
, vol.47
, pp. 6793-6801
-
-
Hakemian, A.S.1
Kondapalli, K.C.2
Telser, J.3
Hoffman, B.M.4
Stemmler, T.L.5
Rosenzweig, A.C.6
-
37
-
-
0036856438
-
Improvement of the puri.cation method for retaining the activity of the particulate methane monooxygenase from Methylosinus trichosporium OB3b
-
Miyaji, A., Kamachi, T. and Okura, I. (2002) Improvement of the puri.cation method for retaining the activity of the particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biotech. Lett. 24, 1883-1887
-
(2002)
Biotech. Lett
, vol.24
, pp. 1883-1887
-
-
Miyaji, A.1
Kamachi, T.2
Okura, I.3
-
38
-
-
1542645043
-
Displacement of iron by zinc at the diiron site of Desulfovibrio vulgaris rubrerythrin: X-ray crystal structure and anomalous scattering analysis
-
Jin, S., Kurtz, Jr, D.M., Liu, Z.-J., Rose, J. and Wang, B.-C. (2004) Displacement of iron by zinc at the diiron site of Desulfovibrio vulgaris rubrerythrin: X-ray crystal structure and anomalous scattering analysis. J. Inorg. Biochem. 98, 786-796
-
(2004)
J. Inorg. Biochem
, vol.98
, pp. 786-796
-
-
Jin, S.1
Kurtz Jr, D.M.2
Liu, Z.-J.3
Rose, J.4
Wang, B.-C.5
-
39
-
-
0035964172
-
Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer
-
Voegtli, W.C., Ge, J., Perlstein, D.L., Stubbe, J. and Rosenzweig, A.C. (2001) Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. Proc. Natl. Acad. Sci. U.S.A. 98, 10073-10078
-
(2001)
Proc. Natl. Acad. Sci. U.S.A
, vol.98
, pp. 10073-10078
-
-
Voegtli, W.C.1
Ge, J.2
Perlstein, D.L.3
Stubbe, J.4
Rosenzweig, A.C.5
|