Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Steven L. Edwards"'
Publikováno v:
Journal of Biological Chemistry. 270:4293-4298
Aromatic amine dehydrogenase (AADH) and methylamine dehydrogenase (MADH) are the only two enzymes known to use the cofactor tryptophan tryptophylquinone (TTQ). Each catalyzes oxidative deamination of a distinct class of primary amines. A detailed com
Autor:
R. Paul Phizackerley, Soichi Wakatsuki, Ian J. Clifton, Janos Hajdu, Steven L. Edwards, James E. Erman, Vilmos Fülöp, S. Michael Soltis
Publikováno v:
Structure. 2:201-208
Background Cytochrome c peroxidase from yeast is a soluble haem- containing protein found in the mitochondrial electron transport chain where it probably protects against toxic peroxides. The aim of this study was to obtain a reliable structure for t
Autor:
Ann M. English, Steven L. Edwards, Giulietta Smulevich, Thomas L. Poulos, Yang Wang, Thomas G. Spiro
Publikováno v:
Biochemistry. 29:2586-2592
Good quality resonance Raman (RR) spectra have been obtained for cytochrome c peroxidase single crystals (0.2 x 0.5 x 1 mm) lying on their 110 faces on a microscope stage. Crystal orientation and polarization effects are observed which differentiate
Publikováno v:
Journal of the American Chemical Society. 113:7755-7757
Autor:
Ted Fox, Thomas L. Poulos, Steven L. Edwards, Gordon Tollin, Ann M. English, James T. Hazzard
Publikováno v:
Journal of the American Chemical Society. 112:7426-7428
Autor:
Limei Hsu Jones, E. Eisenstein, Joann Sanders-Loehr, Andrei Y. Chistoserdov, Shanthi Govindaraj, Victor L. Davidson, Steven L. Edwards
Publikováno v:
Journal of bacteriology. 176(10)
Aromatic amine dehydrogenase (AADH) catalyzes the oxidative deamination of aromatic amines including tyramine and dopamine. AADH is structurally similar to methylamine dehydrogenase (MADH) and possesses the same tryptophan tryptophylquinone (TTQ) pro
The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by usine multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42728e72494ae0d5485ad31e922e71b0
https://europepmc.org/articles/PMC45743/
https://europepmc.org/articles/PMC45743/
Autor:
Victor A. Ashford, J. Matthew Mauro, Joseph Kraut, Stuart J. Oatley, Nguyen Huu Xuong, Jimin Wang, Fishel La, Steven L. Edwards
Publikováno v:
Biochemistry. 29(31)
The 2.2-A X-ray structure for CCP(MI), a plasmid-encoded form of Saccharomyces cerevisiae cytochrome c peroxidase (CCP) expressed in Escherichia coli [Fishel, L.A., Villafranca, J. E., Mauro, J. M.,Kraut, J. (1987) Biochemistry 26, 351-360], has been
Autor:
Mauro Jm, James T. Hazzard, Mark A. Miller, Gordon Tollin, Steven L. Edwards, P C Simons, Joseph Kraut
Publikováno v:
Biochemistry. 27:9081-9088
The long-distance electron transfer observed in the complex formed between ferrocytochrome c and compound I, the peroxide-oxidized form of cytochrome c peroxidase (CCP), has been proposed to occur through the participation of His 181 of CCP and Phe 8
Autor:
Nguyen-Huu Xuong, R A Alden, Joseph Kraut, U Skogland, Steven L. Edwards, B Eriksson, S T Freer, Takashi Yonetani, Thomas L. Poulos, K Takio
Publikováno v:
Journal of Biological Chemistry. 255:575-580