메뉴 건너뛰기




Volumn 21, Issue 2, 2010, Pages 399-404

Metal- and metallocycle-binding sites engineered into polyvalent virus-like scaffolds

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BINDING SITES; CARBON MONOXIDE; ELECTRON TRANSITIONS; METALS; PROTEINS; RATE CONSTANTS; SCAFFOLDS (BIOLOGY); VIRUSES;

EID: 77049102225     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc900399e     Document Type: Article
Times cited : (14)

References (40)
  • 4
    • 38949141867 scopus 로고    scopus 로고
    • Engineering cytochrome P450 enzymes
    • Gillam, E. M. (2008) Engineering cytochrome P450 enzymes. Chem. Res. Toxicol. 21, 220-231.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 220-231
    • Gillam, E.M.1
  • 5
    • 33847030736 scopus 로고    scopus 로고
    • Industrial biotechnology for the production of biobased chemicals - A cradle-to-grave perspective
    • Hatti-Kaul, R., Tornvall, U., Gustaffson, L., and Borjesseon, P. (2007) Industrial biotechnology for the production of biobased chemicals - a cradle-to-grave perspective. Trends Biotechnol. 25, 119-124.
    • (2007) Trends Biotechnol. , vol.25 , pp. 119-124
    • Hatti-Kaul, R.1    Tornvall, U.2    Gustaffson, L.3    Borjesseon, P.4
  • 7
    • 18744377984 scopus 로고    scopus 로고
    • Electrochemical and spectroscopic investigations of immobilized de novo designed heme proteins on metal electrodes
    • Albrecht, T., Li, W., Ulstrup, J., Haehnel, W., and Hildebrandt, P. (2005) Electrochemical and spectroscopic investigations of immobilized de novo designed heme proteins on metal electrodes. ChemPhysChem 6, 961-970.
    • (2005) ChemPhysChem , vol.6 , pp. 961-970
    • Albrecht, T.1    Li, W.2    Ulstrup, J.3    Haehnel, W.4    Hildebrandt, P.5
  • 8
    • 49549085951 scopus 로고    scopus 로고
    • Designed metal-binding sites in biomolecular and bioinorganic interactions
    • Matthews, J. M., Loughlin, F. E., and Mackay, J. P. (2008) Designed metal-binding sites in biomolecular and bioinorganic interactions. Curr. Opin. Struct. Biol. 18, 484-490.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 484-490
    • Matthews, J.M.1    Loughlin, F.E.2    MacKay, J.P.3
  • 10
    • 33748634910 scopus 로고    scopus 로고
    • Biosynthetic inorganic chemistry
    • Lu, Y. (2006) Biosynthetic inorganic chemistry. Angew. Chem., Int. Ed. 45, 5588-5601.
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 5588-5601
    • Lu, Y.1
  • 11
    • 34447636614 scopus 로고    scopus 로고
    • Detection of heme oxygenase activity in a library of four-helix bundle proteins: Towards the de novo synthesis of functional heme proteins
    • Monien, B. H. (2007) Detection of heme oxygenase activity in a library of four-helix bundle proteins: towards the de novo synthesis of functional heme proteins. J. Mol. Biol. 371, 739-753.
    • (2007) J. Mol. Biol. , vol.371 , pp. 739-753
    • Monien, B.H.1
  • 13
    • 51849165035 scopus 로고    scopus 로고
    • Plant viruses as biotemplates for materials and their use in nanotechnology
    • Young, M., Willits, D., Uchida, M., and Douglas, T. (2008) Plant viruses as biotemplates for materials and their use in nanotechnology. Ann. Rev. Phytopathol. 46, 361-384.
    • (2008) Ann. Rev. Phytopathol. , vol.46 , pp. 361-384
    • Young, M.1    Willits, D.2    Uchida, M.3    Douglas, T.4
  • 16
    • 33644928727 scopus 로고    scopus 로고
    • Decoration of cowpea mosaic virus with multiple, redox-active organometallic complexes
    • Steinmetz, N. F., Lomonossoff, G., and Evans, D. J. (2006) Decoration of cowpea mosaic virus with multiple, redox-active organometallic complexes. Small 2, 530-533.
    • (2006) Small , vol.2 , pp. 530-533
    • Steinmetz, N.F.1    Lomonossoff, G.2    Evans, D.J.3
  • 17
    • 66849095549 scopus 로고    scopus 로고
    • M13 bacteriophage as a biological scaffold for magnetically-recoverable metal nanowire catalysts: Combining specific and nonspecific interactions to design multifunctional nanocomposites
    • Avery, K. N., Schaak, J. E., and Schaak, R. E. (2009) M13 bacteriophage as a biological scaffold for magnetically-recoverable metal nanowire catalysts: combining specific and nonspecific interactions to design multifunctional nanocomposites. Chem. Mater. 21, 2176-2178.
    • (2009) Chem. Mater. , vol.21 , pp. 2176-2178
    • Avery, K.N.1    Schaak, J.E.2    Schaak, R.E.3
  • 18
    • 49149088384 scopus 로고    scopus 로고
    • Biomimetic synthesis of beta-TiO2 inside a viral capsid
    • Klem, M. T., Young, M., and Douglas, T. (2008) Biomimetic synthesis of beta-TiO2 inside a viral capsid. J. Mater. Chem. 18, 3821-3823.
    • (2008) J. Mater. Chem. , vol.18 , pp. 3821-3823
    • Klem, M.T.1    Young, M.2    Douglas, T.3
  • 19
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, I., and Belfrage, G. (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258, 598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 20
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides coontaining neighbouring histidine residues
    • Hochuli, E., Dobeli, H., and Schacher, A. (1987) New metal chelate adsorbent selective for proteins and peptides coontaining neighbouring histidine residues. J. Chromatogr. 411, 177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 21
    • 0035979773 scopus 로고    scopus 로고
    • Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins
    • Benson, D. E., Conrad, D. W., de Lorimer, R. M., Trammell, S. A., and Hellinga, H. W. (2001) Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins. Science 293, 1641-1644.
    • (2001) Science , vol.293 , pp. 1641-1644
    • Benson, D.E.1    Conrad, D.W.2    De Lorimer, R.M.3    Trammell, S.A.4    Hellinga, H.W.5
  • 24
    • 55349093907 scopus 로고    scopus 로고
    • Immobilization of bacteriophage Qb on metal-derivatized surfaces via polyvalent display of hexahistidine tags
    • Udit, A. K., Brown, S., Baksh, M. M., and Finn, M. G. (2008) Immobilization of bacteriophage Qb on metal-derivatized surfaces via polyvalent display of hexahistidine tags. J. Inorg. Biochem. 102, 2142-2146.
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 2142-2146
    • Udit, A.K.1    Brown, S.2    Baksh, M.M.3    Finn, M.G.4
  • 28
    • 33747454273 scopus 로고    scopus 로고
    • Characterization of a covalently linked yeast cytochrome c - Cytochrome c peroxidase complex: Evidence for a single catalytically active cytochrome c binding site on cytochrome c peroxidase
    • Nakani, S., Viriyakul, T., Mitchell, R., Vitello, L. B., and Erman, J. E. (2006) Characterization of a covalently linked yeast cytochrome c - cytochrome c peroxidase complex: evidence for a single catalytically active cytochrome c binding site on cytochrome c peroxidase. Biochemistry 45, 9887-9893.
    • (2006) Biochemistry , vol.45 , pp. 9887-9893
    • Nakani, S.1    Viriyakul, T.2    Mitchell, R.3    Vitello, L.B.4    Erman, J.E.5
  • 29
    • 78651165715 scopus 로고
    • The carbon monoxide pigment of liver microsomes
    • Omura, T., and Sato, R. (1964) The carbon monoxide pigment of liver microsomes. J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 30
    • 0006969621 scopus 로고
    • Absorption spectra and some other properties of cytochrome c and of its compounds with ligands
    • Butt, W. D., and Keilin, D. (1962) Absorption spectra and some other properties of cytochrome c and of its compounds with ligands. Proc. R. Soc. London, Ser. B 156, 429-458.
    • (1962) Proc. R. Soc. London, Ser. B , vol.156 , pp. 429-458
    • Butt, W.D.1    Keilin, D.2
  • 31
    • 0001171874 scopus 로고    scopus 로고
    • Voltammetric peak broadening for cytochrome c/alkanethiolate monolayer structures: Dispersion of formal potentials
    • Clark, R. A., and Bowden, E. F. (1997) Voltammetric peak broadening for cytochrome c/alkanethiolate monolayer structures: dispersion of formal potentials. Langmuir 13, 559-565.
    • (1997) Langmuir , vol.13 , pp. 559-565
    • Clark, R.A.1    Bowden, E.F.2
  • 32
    • 33748732441 scopus 로고    scopus 로고
    • Direct electron injection from electrodes to cytochrome P450CAM in biomembrane-like films
    • Zhang, Z., Nassar, A.-E., Lu, Z., Schenkman, J. B., and Rusling, J. F. (1997) Direct electron injection from electrodes to cytochrome P450CAM in biomembrane-like films. J. Chem. Soc., Faraday Trans. 93, 1769-1774.
    • (1997) J. Chem. Soc., Faraday Trans. , vol.93 , pp. 1769-1774
    • Zhang, Z.1    Nassar, A.-E.2    Lu, Z.3    Schenkman, J.B.4    Rusling, J.F.5
  • 33
    • 18744371869 scopus 로고    scopus 로고
    • Active carboxylic acid-terminated alkanethiol self-assembled monolayers on gold bead electrodes for immobilization of cytochromes c
    • Tanimura, R., Hill, M. G., Margoliash, E., Niki, K., Ohno, H., and Gray, H. B. (2002) Active carboxylic acid-terminated alkanethiol self-assembled monolayers on gold bead electrodes for immobilization of cytochromes c. Electrochem. Solid State Lett. 5, E67-E70.
    • (2002) Electrochem. Solid State Lett. , vol.5
    • Tanimura, R.1    Hill, M.G.2    Margoliash, E.3    Niki, K.4    Ohno, H.5    Gray, H.B.6
  • 34
    • 0032583439 scopus 로고    scopus 로고
    • Effects of ligation and folding on reduction potentials of heme proteins
    • Tezcan, F. A., Winkler, J. R., and Gray, H. B. (1998) Effects of ligation and folding on reduction potentials of heme proteins. J. Am. Chem. Soc. 120, 13383-13388.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13383-13388
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 35
    • 49249148639 scopus 로고
    • General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems
    • Laviron, E. (1979) General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems. J. Electroanal. Chem. 101, 19-28.
    • (1979) J. Electroanal. Chem. , vol.101 , pp. 19-28
    • Laviron, E.1
  • 36
    • 20744449130 scopus 로고    scopus 로고
    • Protein-surfactant film voltammetry of wild type and mutant cytochrome P450 BM3
    • Udit, A. K., Hindoyan, N., Hill, M. G., Arnold, F. H., and Gray, H. B. (2005) Protein-surfactant film voltammetry of wild type and mutant cytochrome P450 BM3. Inorg. Chem. 44, 4109-4111.
    • (2005) Inorg. Chem. , vol.44 , pp. 4109-4111
    • Udit, A.K.1    Hindoyan, N.2    Hill, M.G.3    Arnold, F.H.4    Gray, H.B.5
  • 37
    • 4143073628 scopus 로고    scopus 로고
    • Reduction of dioxygen catalyzed by pyrenewired heme domain cytochrome P450 BM3 electrodes
    • Udit, A. K., Hill, M. G., Bittner, V. G., Arnold, F. H., and Gray, H. B. (2004) Reduction of dioxygen catalyzed by pyrenewired heme domain cytochrome P450 BM3 electrodes. J. Am. Chem. Soc. 126, 10218-10219.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10218-10219
    • Udit, A.K.1    Hill, M.G.2    Bittner, V.G.3    Arnold, F.H.4    Gray, H.B.5
  • 38
    • 0000230070 scopus 로고    scopus 로고
    • Novel multinuclear catalysts for the electroreduction of dioxygen directly to water
    • Anson, F. C., Shi, C., and Steiger, B. (1997) Novel multinuclear catalysts for the electroreduction of dioxygen directly to water. Acc. Chem. Res. 30, 437-444.
    • (1997) Acc. Chem. Res. , vol.30 , pp. 437-444
    • Anson, F.C.1    Shi, C.2    Steiger, B.3
  • 39
    • 4043155538 scopus 로고    scopus 로고
    • Targeted proton Delivery in the catalyzed reduction of oxygen to water by bimetallic pacman porphyrins
    • Chang, C. J., Loh, Z.-H., Shi, C., Anson, F. C., and Nocera, D. G. (2004) Targeted proton Delivery in the catalyzed reduction of oxygen to water by bimetallic pacman porphyrins. J. Am. Chem. Soc. 126, 10013-10020.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10013-10020
    • Chang, C.J.1    Loh, Z.-H.2    Shi, C.3    Anson, F.C.4    Nocera, D.G.5
  • 40
    • 33746889054 scopus 로고    scopus 로고
    • Spectroscopy and electrochemistry of cytochrome P450 BM3-surfactant films assemblies
    • Udit, A. K., Hagen, K. D., Gillan, J. M., Goldman, P. J., Star, A., Gray, H. B., and Hill, M. G. (2006) Spectroscopy and electrochemistry of cytochrome P450 BM3-surfactant films assemblies. J. Am. Chem. Soc. 128, 10320-10325.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10320-10325
    • Udit, A.K.1    Hagen, K.D.2    Gillan, J.M.3    Goldman, P.J.4    Star, A.5    Gray, H.B.6    Hill, M.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.