Zobrazeno 1 - 10
of 22
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
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
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
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
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
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
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
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
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
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