Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Celia F. Goodhew"'
Autor:
John A. Shelnutt, Sofia R. Pauleta, Isabel Moura, Graham W. Pettigrew, Celia F. Goodhew, Yi Lu
Publikováno v:
Biochemistry. 47:5841-5850
This work reports for the first time a resonance Raman study of the mixed-valence and fully reduced forms of Paracoccus pantotrophus bacterial cytochrome c peroxidase. The spectra of the active mixed-valence enzyme show changes in the structure of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94bfcd627bcaf2b737fcb840167fba29
https://doi.org/10.1021/bi702486d
https://doi.org/10.1021/bi702486d
Publikováno v:
International Journal of Systematic and Evolutionary Microbiology. 56:2495-2500
An outline of the current taxonomic diversity of the genus Paracoccus is presented. A definitive summary is given of the valid type strains of Paracoccus denitrificans and Paracoccus pantotrophus and of culture collection strains that can be assigned
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::683b3a87804906a7371e48de69c01650
https://doi.org/10.1099/ijs.0.64401-0
https://doi.org/10.1099/ijs.0.64401-0
Autor:
Neil Errington, Stephen E. Harding, Alan Cooper, Margaret Nutley, Celia F. Goodhew, Françoise Guerlesquin, Graham W. Pettigrew, José J. G. Moura, Sofia R. Pauleta, Isabel Moura
Publikováno v:
Biochemistry. 43:14566-14576
Pseudoazurin binds at a single site on cytochrome c peroxidase from Paracoccus pantotrophus with a K(d) of 16.4 microM at 25 degrees C, pH 6.0, in an endothermic reaction that is driven by a large entropy change. Sedimentation velocity experiments co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a8e578319699427f11591165295c996
https://doi.org/10.1021/bi0485833
https://doi.org/10.1021/bi0485833
Autor:
Celia F. Goodhew, Margaret Nutley, Stephen E. Harding, Cristina Costa, José J. G. Moura, Alan Cooper, Kornelia Jumel, Sofia R. Pauleta, Isabel Moura, Ludwig Krippahl, Graham W. Pettigrew
Publikováno v:
Biochemistry. 42:11968-11981
According to the model proposed in previous papers [Pettigrew, G. W., Prazeres, S., Costa, C., Palma, N., Krippahl, L., and Moura, J. J. (1999) The structure of an electron-transfer complex containing a cytochrome c and a peroxidase, J. Biol. Chem. 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fa935e4666e773798542d11e9c0a21e
https://doi.org/10.1021/bi034829c
https://doi.org/10.1021/bi034829c
Autor:
Pedro Tavares, Graham W. Pettigrew, Kornelia Jumel, Steven Harding, Luís C. Duarte, Cristina G. Timóteo, Celia F. Goodhew, Francisco M. Gírio, Isabel Moura
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 8:29-37
The production of cytochrome c peroxidase (CCP) from Pseudomonas ( Ps.) stutzeri (ATCC 11607) was optimized by adjusting the composition of the growth medium and aeration of the culture. The protein was isolated and characterized biochemically and sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22b485a086d12652aa0392d8ebd7cef5
https://doi.org/10.1007/s00775-002-0382-y
https://doi.org/10.1007/s00775-002-0382-y
Autor:
Y. Qiu, Celia F. Goodhew, Sofia R. Pauleta, J. A. Shelnutt, Isabel Moura, Graham W. Pettigrew, Y Lu
Publikováno v:
Journal of Inorganic Biochemistry. 86:381-390
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0dd2b30d5dceb87a23faf1987dabbc68
https://doi.org/10.1016/s0162-0134(01)00285-9
https://doi.org/10.1016/s0162-0134(01)00285-9
Autor:
Cristina Costa, J. Van Beeumen, Ludwig Krippahl, José J. G. Moura, Bart Devreese, Celia F. Goodhew, Raymond Gilmour, Graham W. Pettigrew, Dominic J. B. Hunter, Isabel Moura, Susana Prazeres, P. N. Palma
Publikováno v:
European Journal of Biochemistry. 258:559-566
The implications of the dimeric state of cytochrome c550 for its binding to Paracoccus cytochrome c peroxidase and its delivery of the two electrons required to restore the active enzyme during catalysis have been investigated. The amino acid sequenc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d7e94d7d957e02a3286ff1bdf2aeb8a
https://doi.org/10.1046/j.1432-1327.1998.2580559.x
https://doi.org/10.1046/j.1432-1327.1998.2580559.x
Autor:
Ian P. Thompson, Graham W. Pettigrew, Rob J.M. van Spanning, Jozef Van Beeumen, Neil F. W. Saunders, Simon C. Baker, Celia F. Goodhew, Stuart J. Ferguson, Bart Devreese
Publikováno v:
FEMS Microbiology Letters. 137:95-101
The c-type cytochrome and protein profiles were compared for a number of cultures of Paracoccus denitrificans obtained from a range of culture collections. The cultures fell into two groups corresponding to the two original isolates of this bacterial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30b1980f64d8735620bdf757a54e7b0b
https://doi.org/10.1111/j.1574-6968.1996.tb08089.x
https://doi.org/10.1111/j.1574-6968.1996.tb08089.x
Autor:
Celia F. Goodhew, Isabel Moura, Susana Prazeres, Natarajan Ravi, Raymond Gilmour, Boi Hanh Huynh, José J. G. Moura, Graham W. Pettigrew
Publikováno v:
Journal of Biological Chemistry. 270:24264-24269
Mossbauer and electron paramagnetic resonance (EPR) spectroscopies were used to characterize the diheme cytochrome c peroxidase from Paracoccus denitrificans (L.M.D. 52.44). The spectra of the oxidized enzyme show two distinct spectral components cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccbc5dc22a54f0a3dda8da0ecfb1281d
https://doi.org/10.1074/jbc.270.41.24264
https://doi.org/10.1074/jbc.270.41.24264
Autor:
Susana Prazeres, Celia F. Goodhew, Raymond Gilmour, Isabel Moura, José J. G. Moura, Graham W. Pettigrew
Publikováno v:
Magnetic Resonance in Chemistry. 31:S68-S72
Cytochrome c peroxidase from Paracoccus denitrificans LMD 52.44 was recently identified. The enzyme contains two c-type haems: one is reducible physiologically by cytochrome c550 from the same organism or non-physiologically by ascorbate (high-potent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d9c31ffc90c5dfc91dcacd0d8b7ef5a
https://doi.org/10.1002/mrc.1260311314
https://doi.org/10.1002/mrc.1260311314