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Structural consequences of effector protein complex formation in a diiron hydroxylase.

Bailey LJ, McCoy JG, Phillips GN, Fox BG
Proc Natl Acad Sci U S A 105 19194-8 (2008)
Related entries: 3dhg, 3dhh

Cited: 61 times
EuropePMC logo PMID: 19033467

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 A 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.

Reviews - 3dhi mentioned but not cited (1)

  1. Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes. Jasniewski AJ, Que L. Chem. Rev. 118 2554-2592 (2018)

Articles - 3dhi mentioned but not cited (6)

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