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Title: Structural consequences of effector protein complex formation in a diiron hydroxylase

Abstract

Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 {angstrom} from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.

Authors:
; ;  [1]
  1. UW
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1007087
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. USA
Additional Journal Information:
Journal Volume: 105; Journal Issue: (49) ; 12, 2008; Journal ID: ISSN 0027-8424
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; BIOREMEDIATION; CATABOLISM; CATALYSIS; ENZYMES; FUNCTIONALS; HYDROCARBONS; HYDROXYLASES; MOLECULAR WEIGHT; PROTEINS; SYNTHESIS; TOLUENE

Citation Formats

Bailey, Lucas J, McCoy, Jason G, Phillips, Jr., George N., and Fox, Brian G. Structural consequences of effector protein complex formation in a diiron hydroxylase. United States: N. p., 2009. Web. doi:10.1073/pnas.0807948105.
Bailey, Lucas J, McCoy, Jason G, Phillips, Jr., George N., & Fox, Brian G. Structural consequences of effector protein complex formation in a diiron hydroxylase. United States. https://doi.org/10.1073/pnas.0807948105
Bailey, Lucas J, McCoy, Jason G, Phillips, Jr., George N., and Fox, Brian G. Fri . "Structural consequences of effector protein complex formation in a diiron hydroxylase". United States. https://doi.org/10.1073/pnas.0807948105.
@article{osti_1007087,
title = {Structural consequences of effector protein complex formation in a diiron hydroxylase},
author = {Bailey, Lucas J and McCoy, Jason G and Phillips, Jr., George N. and Fox, Brian G},
abstractNote = {Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 {angstrom} from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.},
doi = {10.1073/pnas.0807948105},
url = {https://www.osti.gov/biblio/1007087}, journal = {Proc. Natl. Acad. Sci. USA},
issn = {0027-8424},
number = (49) ; 12, 2008,
volume = 105,
place = {United States},
year = {2009},
month = {6}
}