Structural consequences of effector protein complex formation in a diiron hydroxylase

Journal Article · Fri Jun 12 04:00:00 EDT 2009 · Proc. Natl. Acad. Sci. USA

DOI:https://doi.org/10.1073/pnas.0807948105· OSTI ID:1007087

Bailey, Lucas J; McCoy, Jason G; Fox, Brian G ^[1]

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1. UW

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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1007087
• Journal Information: Proc. Natl. Acad. Sci. USA, Journal Name: Proc. Natl. Acad. Sci. USA Journal Issue: (49) ; 12, 2008 Vol. 105; ISSN PNASA6; ISSN 0027-8424
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
BIOREMEDIATION
CATABOLISM
CATALYSIS
ENZYMES
FUNCTIONALS
HYDROCARBONS
HYDROXYLASES
MOLECULAR WEIGHT
PROTEINS
SYNTHESIS
TOLUENE