-
1
-
-
0035903128
-
The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
-
Outten, F. W., Huffman, D. L., Hale, J. A., and O'Halloran, T. V. (2001) The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J. Biol. Chem. 276, 30670-30677.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 30670-30677
-
-
Outten, F.W.1
Huffman, D.L.2
Hale, J.A.3
O'Halloran, T.V.4
-
2
-
-
0037022682
-
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli
-
DOI 10.1073/pnas.052710499
-
Roberts, S. A., Weichsel, A., Grass, G., Thakali, K., Hazzard, J. T., Tollin, G., Rensing, C., and Montfort, W. R. (2002) Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. U.S. A. 99, 2766-2771. (Pubitemid 34240535)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.5
, pp. 2766-2771
-
-
Roberts, S.A.1
Weichsel, A.2
Grass, G.3
Thakali, K.4
Hazzard, J.T.5
Tollin, G.6
Rensing, C.7
Montfort, W.R.8
-
3
-
-
0041856135
-
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO
-
DOI 10.1074/jbc.M302963200
-
Roberts, S. A., Wildner, G. F., Grass, G., Weichsel, A., Ambrus, A., Rensing, C., and Montfort, W. R. (2003) A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO. J. Biol. Chem. 278, 31958-31963. (Pubitemid 37048383)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.34
, pp. 31958-31963
-
-
Roberts, S.A.1
Wildner, G.F.2
Grass, G.3
Weichsel, A.4
Ambrus, A.5
Rensing, C.6
Montfort, W.R.7
-
4
-
-
4344580278
-
Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli
-
DOI 10.1128/JB.186.17.5826-5833.2004
-
Grass, G., Thakali, K., Klebba, P. E., Thieme, D., Muller, A., Wildner, G. F., and Rensing, C. (2004) Linkage between catecholate siderophores and multicopper oxidase CueO in Escherichia coli. J. Bacteriol. 186, 5826-5833. (Pubitemid 39128656)
-
(2004)
Journal of Bacteriology
, vol.186
, Issue.17
, pp. 5826-5833
-
-
Grass, G.1
Thakali, K.2
Klebba, P.E.3
Thieme, D.4
Muller, A.5
Wildner, G.F.6
Rensing, C.7
-
5
-
-
7744237723
-
Cuprous oxidase activity of CueO from Escherichia coli
-
DOI 10.1128/JB.186.22.7815-7817.2004
-
Singh, S. K., Grass, G., Rensing, C., and Montfort, W. R. (2004) Cuprous oxidase activity of CueO from Escherichia coli. J. Bacteriol. 186, 7815-7817. (Pubitemid 39463750)
-
(2004)
Journal of Bacteriology
, vol.186
, Issue.22
, pp. 7815-7817
-
-
Singh, S.K.1
Grass, G.2
Rensing, C.3
Montfort, W.R.4
-
6
-
-
33745870084
-
Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen
-
DOI 10.1016/j.febslet.2006.06.049, PII S0014579306007642
-
Ueki, Y., Inoue, M., Kurose, S., Kataoka, K., and Sakurai, T. (2006) Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen. FEBS Lett. 580, 4069-4072. (Pubitemid 44037572)
-
(2006)
FEBS Letters
, vol.580
, Issue.17
, pp. 4069-4072
-
-
Ueki, Y.1
Inoue, M.2
Kurose, S.3
Kataoka, K.4
Sakurai, T.5
-
7
-
-
67649771937
-
506located adjacent to the trinuclear copper center
-
506located adjacent to the trinuclear copper center. J. Biol. Chem. 284, 14405-14413.
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 14405-14413
-
-
Kataoka, K.1
Sugiyama, R.2
Hirota, S.3
Inoue, M.4
Urata, K.5
Minagawa, Y.6
Seo, D.7
Sakurai, T.8
-
8
-
-
77956928109
-
ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase
-
Iwaki, M., Kataoka, K., Kajino, T., Sugiyama, R., Morishita, H., and Sakurai, T. (2010) ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase. FEBS Lett. 584, 4027-4031.
-
(2010)
FEBS Lett.
, vol.584
, pp. 4027-4031
-
-
Iwaki, M.1
Kataoka, K.2
Kajino, T.3
Sugiyama, R.4
Morishita, H.5
Sakurai, T.6
-
9
-
-
34848846870
-
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
-
Sakurai, T., and Kataoka, K. (2007) Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem. Rec. 7, 220-229.
-
(2007)
Chem. Rec.
, vol.7
, pp. 220-229
-
-
Sakurai, T.1
Kataoka, K.2
-
10
-
-
35648965701
-
Structure and function of type I copper in multicopper oxidases
-
DOI 10.1007/s00018-007-7183-y
-
Sakurai, T., and Kataoka, K. (2007) Structure and function of type I copper in multicopper oxidases. Cell. Mol. Life Sci. 64, 2642-2656. (Pubitemid 350035609)
-
(2007)
Cellular and Molecular Life Sciences
, vol.64
, Issue.19-20
, pp. 2642-2656
-
-
Sakurai, T.1
Kataoka, K.2
-
11
-
-
34548557237
-
Structure and Function of the Engineered Multicopper Oxidase CueO from Escherichia coli-Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site
-
DOI 10.1016/j.jmb.2007.07.041, PII S0022283607009692
-
Kataoka, K., Komori, H., Ueki, Y., Konno, Y., Kamitaka, Y., Kurose, S., Tsujimura, S., Higuchi, Y., Kano, K., Seo, D., and Sakurai, T. (2007) Structure and function of the engineered multicopper oxidase CueO from Escherichia coli: Deletion of the methionine- rich helical region covering the substrate-binding site. J. Mol. Biol. 373, 141-152 (Pubitemid 47390714)
-
(2007)
Journal of Molecular Biology
, vol.373
, Issue.1
, pp. 141-152
-
-
Kataoka, K.1
Komori, H.2
Ueki, Y.3
Konno, Y.4
Kamitaka, Y.5
Kurose, S.6
Tsujimura, S.7
Higuchi, Y.8
Kano, K.9
Seo, D.10
Sakurai, T.11
-
12
-
-
34247198442
-
Promotion of laccase activities of Escherichia coli cuprous oxidase, CueO by deleting the segment covering the substrate binding site
-
Kurose, S., Kataoka, K., Otsuka, K., Tsujino, Y., and Sakurai, T. (2007) Promotion of laccase activities of Escherichia coli cuprous oxidase, CueO by deleting the segment covering the substrate binding site. Chem. Lett. 36, 232-233.
-
(2007)
Chem. Lett.
, vol.36
, pp. 232-233
-
-
Kurose, S.1
Kataoka, K.2
Otsuka, K.3
Tsujino, Y.4
Sakurai, T.5
-
13
-
-
65249109256
-
Modification of spectroscopic properties and catalytic activity of Escherichia coli CueO by mutations of methionine 510, the axial ligand to the type i Cu
-
Kurose, S., Kataoka, K., Shinohara, N., Miura, Y., Tsutsumi, M., Tsujimura, S., Kano, K., and Sakurai, T. (2009) Modification of spectroscopic properties and catalytic activity of Escherichia coli CueO by mutations of methionine 510, the axial ligand to the type I Cu. Bull. Chem. Soc. Jpn. 82, 504-508.
-
(2009)
Bull. Chem. Soc. Jpn.
, vol.82
, pp. 504-508
-
-
Kurose, S.1
Kataoka, K.2
Shinohara, N.3
Miura, Y.4
Tsutsumi, M.5
Tsujimura, S.6
Kano, K.7
Sakurai, T.8
-
14
-
-
33846678076
-
Ceruloplasmin revisited: Structural and functional roles of various metal cation-binding sites
-
DOI 10.1107/S090744490604947X
-
Bento, I., Peixoto, C., Zaitzev, V. N., and Lindley, P. F. (2007) Ceruloplasmin revised: Structural and functional roles of various metal cation-binding sites. Acta Crystallogr. D63, 240-248. (Pubitemid 46197541)
-
(2007)
Acta Crystallographica Section D: Biological Crystallography
, vol.63
, Issue.2
, pp. 240-248
-
-
Bento, I.1
Peixoto, C.2
Zaitsev, V.N.3
Lindley, P.F.4
-
15
-
-
60849101381
-
Direct electrochemistry of CueO and its mutants at residues to and from near type i Cu for oxygen-reducing biocathode
-
Miura, Y., Tsujimura, S., Kurose, S., Kataoka, K., Sakurai, T., and Kano, K. (2009) Direct electrochemistry of CueO and its mutants at residues to and from near type I Cu for oxygen-reducing biocathode. Fuel Cells 9, 70-78.
-
(2009)
Fuel Cells
, vol.9
, pp. 70-78
-
-
Miura, Y.1
Tsujimura, S.2
Kurose, S.3
Kataoka, K.4
Sakurai, T.5
Kano, K.6
-
16
-
-
0036185564
-
An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
-
DOI 10.1016/S0162-0134(02)00364-1, PII S0162013402003641
-
Machczynski, M. C., Gray, H. B., and Richards, J. H. (2002) An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins. J. Inorg. Biochem. 88, 375-380. (Pubitemid 34207850)
-
(2002)
Journal of Inorganic Biochemistry
, vol.88
, Issue.3-4
, pp. 375-380
-
-
Machczynski, M.C.1
Gray, H.B.2
Richards, J.H.3
-
17
-
-
3242666035
-
Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper
-
DOI 10.1021/bi049634z
-
Carrell, C. J., Sun, D., Jiang, S., Davidson, V. L., and Mathews, F. S. (2004) Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper. Biochemistry 43, 9372-9380. (Pubitemid 38955470)
-
(2004)
Biochemistry
, vol.43
, Issue.29
, pp. 9372-9380
-
-
Carrell, C.J.1
Sun, D.2
Jiang, S.3
Davidson, V.L.4
Mathews, F.S.5
-
18
-
-
0026525991
-
Site-directed mutagenesis of pseudoazurin from Alcaligenes faecalis S-6; Pro80Ala mutant exhibits marked increase in reduction potential
-
Nishiyama, M., Suzuki, J., Ohnuki, T., Chan, H. C., Horinouchi, S., Turley, S., Adman, E. T., and Beppu, T. (1992) Site-directed mutagenesis of pseudoazurin from Alcaligenes faecalis S-6; Pro80Ala mutant exhibits marked increase in reduction potential. Protein Eng. 5, 177-184.
-
(1992)
Protein Eng.
, vol.5
, pp. 177-184
-
-
Nishiyama, M.1
Suzuki, J.2
Ohnuki, T.3
Chan, H.C.4
Horinouchi, S.5
Turley, S.6
Adman, E.T.7
Beppu, T.8
-
19
-
-
33746223994
-
The role of hydrogen bonding at the active site of a cupredoxin: The Phe114Pro azurin variant
-
DOI 10.1021/bi0606851
-
Yanagisawa, S., Banfield, M. J., and Dennison, C. (2006) The role of hydrogen bonding at the active site of a cupredoxin: The Phe114Pro azurin variant. Biochemistry 45, 8812-8822. (Pubitemid 44100677)
-
(2006)
Biochemistry
, vol.45
, Issue.29
, pp. 8812-8822
-
-
Yanagisawa, S.1
Banfield, M.J.2
Dennison, C.3
-
20
-
-
70449090691
-
Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
-
Marshall, N. M., Garner, D. K., Wilson, T. D., Gao, Y. G., Robinson, H., Nilges, M. J., and Lu, Y. (2009) Rationally tuning the reduction potential of a single cupredoxin beyond the natural range. Nature 462, 113-116.
-
(2009)
Nature
, vol.462
, pp. 113-116
-
-
Marshall, N.M.1
Garner, D.K.2
Wilson, T.D.3
Gao, Y.G.4
Robinson, H.5
Nilges, M.J.6
Lu, Y.7
-
21
-
-
0026355316
-
Resonance raman spectra of plastocyanin and pseudoazurin: Evidence for conserved cysteine ligand conformations in cupredoxins (blue copper proteins)
-
Han, J., Adman, E. T., Beppu, T., Codd, R., Freeman, H. C., Huq, L. L., Loehr, T. M., and Sanders-Loehr, J. (1991) Resonance Raman spectra of plastocyanin and pseudoazurin: Evidence for conserved cysteine ligand conformations in cupredoxins (blue copper proteins). Biochemistry 30, 10904-10913.
-
(1991)
Biochemistry
, vol.30
, pp. 10904-10913
-
-
Han, J.1
Adman, E.T.2
Beppu, T.3
Codd, R.4
Freeman, H.C.5
Huq, L.L.6
Loehr, T.M.7
Sanders-Loehr, J.8
-
22
-
-
38549152785
-
Diffusion-controlled oxygen reduction on multi-copper oxidase-adsorbed carbon aerogel electrodes without mediator
-
DOI 10.1002/fuce.200700032
-
Tsujimura, S., Kamitaka, Y., and Kano, K. (2007) Diffusion-controlled oxygen reduction on multi-copper oxidase-adsorbed on carbon aerogel electrodes without mediator. Fuel Cells 7, 463-469. (Pubitemid 351160403)
-
(2007)
Fuel Cells
, vol.7
, Issue.6
, pp. 463-469
-
-
Tsujimura, S.1
Kamitaka, Y.2
Kano, K.3
-
23
-
-
43049139480
-
CueO-immobilized porous carbon electrode exhibiting improved performance of electrochemical reduction of dioxygen to water
-
Tsujimura, S., Miura, Y., and Kano, K. (2008) CueO-immobilized porous carbon electrode exhibiting improved performance of electrochemical reduction of dioxygen to water. Electrochim. Acta 53, 5716-5720.
-
(2008)
Electrochim. Acta
, vol.53
, pp. 5716-5720
-
-
Tsujimura, S.1
Miura, Y.2
Kano, K.3
-
24
-
-
18144407596
-
Direct electron transfer between copper-containing proteins and electrodes
-
DOI 10.1016/j.bios.2004.10.003, 20th Anniversary of Biosendors and Bioelectronics
-
Shleev, S., Tkac, J., Christenson, A., Ruzgas, T., Yaropolov, A. I., Whittaker, J. W., and Gorton, L. (2005) Direct electron transfer between copper-containing proteins and electrodes. Biosens. Bioelectron. 20, 2517-2554. (Pubitemid 40613011)
-
(2005)
Biosensors and Bioelectronics
, vol.20
, Issue.12
, pp. 2517-2554
-
-
Shleev, S.1
Tkac, J.2
Christenson, A.3
Ruzgas, T.4
Yaropolov, A.I.5
Whittaker, J.W.6
Gorton, L.7
-
25
-
-
49049118534
-
Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis
-
Cracknell, J. A., Vincent, K. A., and Armstrong, F. A. (2008) Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. Chem. Rev. 108, 2439-2461.
-
(2008)
Chem. Rev.
, vol.108
, pp. 2439-2461
-
-
Cracknell, J.A.1
Vincent, K.A.2
Armstrong, F.A.3
-
26
-
-
0032931026
-
Site-directed mutagenesis of a possible type I copper ligand of bilirubin oxidase; a Met467Gln mutant shows stellacyanin-like properties
-
Shimizu, A., Sasaki, T., Kwon, J.-H., Odaka, A., Satoh, T., Sakurai, N., Sakurai, T., Yamaguchi, S., and Samejima, T. (1999) Site-directed mutagenesis of a possible type I copper ligand of bilirubin oxidase; a Met467Gln mutant shows stellacyanin-like properties. J. Biochem. 125, 662-668. (Pubitemid 29192485)
-
(1999)
Journal of Biochemistry
, vol.125
, Issue.4
, pp. 662-668
-
-
Shimizu, A.1
Sasaki, T.2
Kwon, J.H.3
Odaka, A.4
Satoh, T.5
Sakurai, N.6
Sakurai, T.7
Yamaguchi, S.8
Samejima, T.9
-
27
-
-
0033537661
-
Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands
-
Shimizu, A., Kwon, J.-H., Sasaki, T., Satoh, T., Sakurai, N., Sakurai, T., Yamaguchi, S., and Samejima, T. (1999) Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands. Biochemistry 38, 3034-3042.
-
(1999)
Biochemistry
, vol.38
, pp. 3034-3042
-
-
Shimizu, A.1
Kwon, J.-H.2
Sasaki, T.3
Satoh, T.4
Sakurai, N.5
Sakurai, T.6
Yamaguchi, S.7
Samejima, T.8
-
28
-
-
33644882219
-
The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin
-
Sakurai, T. (2006) The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin. FEBS Lett. 580, 1729-1732.
-
(2006)
FEBS Lett.
, vol.580
, pp. 1729-1732
-
-
Sakurai, T.1
-
29
-
-
0030512439
-
Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: Crystal structures and spectral properties
-
DOI 10.1107/S0907444996004982
-
Tsai, L. C., Bonander, N., Harata, K., Karlsson, G., Vanngard, T., Langer, V., and Sjolin, L. (1996) Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: Crystal structures and spectral properties. Acta Crystallogr. D52, 950-958. (Pubitemid 27064198)
-
(1996)
Acta Crystallographica Section D: Biological Crystallography
, vol.52
, Issue.5
, pp. 950-958
-
-
Tsai, L.-C.1
Bonander, N.2
Harata, K.3
Karlsson, G.4
Vanngard, T.5
Langer, V.6
Sjolin, L.7
-
30
-
-
3042694367
-
Determinants of the relative reduction potentials of type-1 copper sites in proteins
-
DOI 10.1021/ja049345y
-
Li, H., Webb, S. P., Ivanic, J., and Jensen, J. H. (2004) Determinants of the relative reduction potential of type-1 copper sites in proteins. J. Am. Chem. Soc. 126, 8010-8019. (Pubitemid 38812793)
-
(2004)
Journal of the American Chemical Society
, vol.126
, Issue.25
, pp. 8010-8019
-
-
Li, H.1
Webb, S.P.2
Ivanic, J.3
Jensen, J.H.4
-
31
-
-
0037473550
-
Frozen density functional free energy simulations of redox proteins: Computational studies of the reduction potential of plastocyanin and rusticyanin
-
Olsson, M. H. M., Hong, G., and Warshel, A. (2003) Frozen density functional free energy simulations of redox proteins: Computational studies of the reduction potential of plastocyanin and rusticyanin J. Am. Chem. Soc. 125, 5025-5039. (Pubitemid 36520432)
-
(2003)
Journal of the American Chemical Society
, vol.125
, Issue.17
, pp. 5025-5039
-
-
Olsson, M.H.M.1
Hong, G.2
Warshel, A.3
-
32
-
-
33750310022
-
Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p
-
DOI 10.1021/bi061543+
-
Stoj, C. S., Augustine, A. J., Zeigler, L., Solomon, E. I., and Kosman, D. J. (2006) Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p. Biochemistry 45, 12741-12749. (Pubitemid 44630860)
-
(2006)
Biochemistry
, vol.45
, Issue.42
, pp. 12741-12749
-
-
Stoj, C.S.1
Augustine, A.J.2
Zeigler, L.3
Solomon, E.I.4
Kosman, D.J.5
|