Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jeremie D. Pikus"'
Autor:
Jurgen F. Doreleijers, Luke A. Moe, John L. Markley, Brian F. Volkman, William M. Westler, Francis C. Peterson, Lars Skjeldal, Brian G. Fox, Jeremie D. Pikus
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 9:945-953
Toluene 4-monooxygenase, a four-protein complex from Pseudomonas mendocina KR1, catalyzes the NADH- and O(2)-dependent hydroxylation of toluene to form p-cresol. The solution structure of the 112-amino-acid Rieske ferredoxin component, T4moC, was det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40291aa969035a450b2e806af75c8364
https://doi.org/10.1007/s00775-004-0594-4
https://doi.org/10.1007/s00775-004-0594-4
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 8:318-326
The diiron ferredoxins have a common diamond-core structure with two bridging sulfides, but differ in the nature of their terminal ligands: either four cysteine thiolates in the Fe(2)S(2) ferredoxins or two cysteine thiolates and two histidine imidaz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f8fa5fbc53031d0f8bdeeca3f28bce
https://doi.org/10.1007/s00775-002-0417-4
https://doi.org/10.1007/s00775-002-0417-4
Autor:
Joey M. Studts, Jeremie D. Pikus, Brian G. Fox, Robert J. Steffan, Kevin H. Mitchell, Kevin McClay
Publikováno v:
Biochemistry. 39:791-799
The diiron enzyme toluene 4-monooxygenase from Pseudomonas mendocina KR1 catalyzes the NADH- and O(2)-dependent hydroxylation of toluene. A combination of sequence alignments and spectroscopic studies indicate that T4MO has an active site structure c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ad06a9baee1e7a7ac9ba5d0db2d8dd4
https://doi.org/10.1021/bi992187g
https://doi.org/10.1021/bi992187g
Autor:
Jeremie D. Pikus, Kevin McClay, Karl Kauffmann, Eckard Münck, Brian G. Fox, Catalina Achim, Robert J. Steffan, Joey M. Studts
Publikováno v:
Biochemistry. 35:9106-9119
Expression of the tmoA-F gene cluster from Pseudomonas mendocina KRI in Escherichia coli BL21(DE3) produces a catalytically active form of the toluene-4-monooxygenase (T4MO) complex. Here we report the purification and characterization of four solubl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ad395f49b7b18655c37c38c138f84f1
https://doi.org/10.1021/bi960456m
https://doi.org/10.1021/bi960456m
Autor:
Kevin H. Mitchell, Jeremie D. Pikus, Kevin McClay, Joey M. Studts, Brian G. Fox, Robert J. Steffan
Publikováno v:
Protein expression and purification. 20(1)
Toluene 4-monooxygenase is a four-protein complex that catalyzes the O 2 - and NADH-dependent oxidation of toluene to p -cresol. The influence of various expression systems on the host cell growth characteristics, purified protein yields, and specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86692e1ce4903484be46964bf6adbc23
https://pubmed.ncbi.nlm.nih.gov/11035951
https://pubmed.ncbi.nlm.nih.gov/11035951
Autor:
Robert J. Steffan, William M. Westler, Kevin McClay, Jeremie D. Pikus, Young Kee Chae, Weidong Xia, Brian G. Fox, John L. Markley, Bin Xia
Publikováno v:
Biochemistry. 38(2)
T4MOC is a 12.3 kDa soluble Rieske ferredoxin that is obligately required for electron transfer between the oxidoreductase and diiron hydroxylase components of toluene 4-monooxygenase from Pseudomonas mendocina KR1. Our preliminary 1H NMR studies of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b335ad0295e112f975a47d2164d956b
https://pubmed.ncbi.nlm.nih.gov/9888813
https://pubmed.ncbi.nlm.nih.gov/9888813
Publikováno v:
Biochemistry. 36(31)
Pseudomonas mendocina KR1 toluene 4-monooxygenase is a multicomponent diiron enzyme. the diiron center is contained in the tmoA polypeptide of teh hydroxylase component [alphabetagamma)2,Mr approximately 212 kDa]. Product distribution studies reveal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f663f00fe53b37fb634cdf69736f2af5
https://pubmed.ncbi.nlm.nih.gov/9280437
https://pubmed.ncbi.nlm.nih.gov/9280437
Publikováno v:
Journal of Biomolecular NMR. 21:73-74
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1b5daa2e0a4736896d74f150068f648
https://doi.org/10.1023/a:1011924200884
https://doi.org/10.1023/a:1011924200884