Molecular bases of electron transport component selectivity in aromatic ring-hydroxylating dioxygenase system

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Crystal structures of reduced form of ferredoxin component (Fd) and complex form of oxidized Fd and reduced oxygenase (Oxy) of carbazole 1,9a-dioxygeanse were solved. Cleavages of salt-bridge between Oxy R118 and Fd E43 and hydrogen-bonding between Oxy R210 and Fd E55 were detected along with the reduction of Oxy. Alanine replacement analyses revealed these bindings are cooperatively enhanced the binding between Oxy and Fd. Isothermal titration calorimetry analyses also revealed that the binding through hydrophobic interaction between the components were stabilized by surrounding salt-bridge and hydrogen-bonding.