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Title: X-Ray Structure of a Hydroxylase-Regulatory Protein Complex From a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas Sp. OX1 Phenol Hydroxylase

Abstract

No abstract prepared.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org.:
USDOE
OSTI Identifier:
898872
Report Number(s):
SLAC-REPRINT-2006-203
TRN: US200706%%393
DOE Contract Number:
AC02-76SF00515
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochem.45:15392-15404,2006
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; HYDROXYLASES; PHENOL; PROTEINS; PSEUDOMONAS; Other,OTHER

Citation Formats

Sazinsky, M.H., Dunten, P.W., McCormick, M.S., DiDonato, A., Lippard, S.J., and /MIT /SLAC, SSRL /Naples U.. X-Ray Structure of a Hydroxylase-Regulatory Protein Complex From a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas Sp. OX1 Phenol Hydroxylase. United States: N. p., 2007. Web.
Sazinsky, M.H., Dunten, P.W., McCormick, M.S., DiDonato, A., Lippard, S.J., & /MIT /SLAC, SSRL /Naples U.. X-Ray Structure of a Hydroxylase-Regulatory Protein Complex From a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas Sp. OX1 Phenol Hydroxylase. United States.
Sazinsky, M.H., Dunten, P.W., McCormick, M.S., DiDonato, A., Lippard, S.J., and /MIT /SLAC, SSRL /Naples U.. Fri . "X-Ray Structure of a Hydroxylase-Regulatory Protein Complex From a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas Sp. OX1 Phenol Hydroxylase". United States. doi:.
@article{osti_898872,
title = {X-Ray Structure of a Hydroxylase-Regulatory Protein Complex From a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas Sp. OX1 Phenol Hydroxylase},
author = {Sazinsky, M.H. and Dunten, P.W. and McCormick, M.S. and DiDonato, A. and Lippard, S.J. and /MIT /SLAC, SSRL /Naples U.},
abstractNote = {No abstract prepared.},
doi = {},
journal = {Biochem.45:15392-15404,2006},
number = ,
volume = ,
place = {United States},
year = {Fri Feb 02 00:00:00 EST 2007},
month = {Fri Feb 02 00:00:00 EST 2007}
}
  • Toluene/o-xylene monooxygenase (ToMO) from Pseudomonas stutzeri OX1, which oxidizes toluene and o-xylene, was examined for its ability to degrade the environmental pollutants trichloroethylene (TCE), 1,1-dichloroethylene (1,1-DCE), cis-1,2-DCE, trans-1,2-DCE, chloroform, dichloromethane, phenol, 2,4-dichlorophenol, 2,4,5-trichlorophenol, 2,4,6-trichlorophenol, 2,3,5,6-tetrachlorophenol, and 2,3,4,5,6-pentachlorophenol. Escherichia coli JM109 that expressed ToMO from genes on plasmid pBZ1260 under control of the lac promoter degraded TCE, 1,1-DCE, and chloroform at initial rates of 3.1, 3.6, and 1.6 nmol, respectively. Stoichiometric amounts of chloride release were seen, indicating mineralization. Thus, the substrate range of ToMO is extended to include aliphatic chlorinated compounds.
  • The toluene/o-xylene monooxygenase cloned from Pseudomonas stutzeri OX1 displays a very broad range of substrates and a very peculiar regioselectivity, because it is able to hydroxylate more than one position on the aromatic ring of several hydrocarbons and phenols. The nucleotide sequence of the gene cluster coding for this enzymatic system has been determined. The sequence analysis revealed the presence of six open reading frames (ORFs) homologous to other genes clustered in operons coding for multicomponent monooxygenases found in benzene- and toluene-degradative pathways cloned from Pseudomonas strains. Significant similarities were also found with multicomponent monooxygenase systems for phenol, methane, alkene,more » and dimethyl sulfide cloned from different bacterial strains. The knockout of each ORF and complementation with the wild-type allele indicated that all six ORFs are essential for the full activity of the toluene/o-xylene monooxygenase in Escherichia coli. This analysis also shows that despite its activity on both hydrocarbons and phenols, toluene/o-xylene monooxygenase belongs to a toluene multicomponent monooxygenase subfamily rather than to the monooxygenases active on phenols.« less
  • The complex of NADH and 3α-HSD from Pseudomonas sp. B-0831 has been crystallized and X-ray diffraction data have been collected to 1.8 Å resolution. The NAD(P){sup +}-dependent enzyme 3α-hydroxysteroid dehydrogenase (3α-HSD) catalyzes the reversible interconversion of hydroxyl and oxo groups at position 3 of the steroid nucleus. The complex of NADH and 3α-HSD from Pseudomonas sp. B-0831 was crystallized by the hanging-drop vapour-diffusion method. Refinement of crystallization conditions with microseeding improved the quality of the X-ray diffraction data to a resolution of 1.8 Å. The crystals belonged to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters amore » = 62.46, b = 82.25, c = 86.57 Å, and contained two molecules, reflecting dimer formation of 3α-HSD, in the asymmetric unit.« less
  • No abstract prepared.