4HJL

Naphthalene 1,2-Dioxygenase bound to 1-chloronaphthalene

Summary for 4HJL

• Entry DOI: 10.2210/pdb4hjl/pdb
• Related: 1EG9 1NDO 1O7G 1O7H 1O7M 1O7N 1O7P 1O7W 1UUV 1UUW 2HMJ 2HMK 2HML 2HMM 2HMN 2HMO
• Descriptor: Naphthalene 1,2-dioxygenase subunit alpha, Naphthalene 1,2-dioxygenase subunit beta, FE2/S2 (INORGANIC) CLUSTER, ... (8 entities in total)
• Functional Keywords: oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor
• Biological source: Pseudomonas sp.; More
• Total number of polymer chains: 2
• Total formula weight: 73272.74

Authors

Ferraro, D.J.,Ramaswamy, S. (deposition date: 2012-10-12, release date: 2013-10-16, Last modification date: 2024-11-06)

Primary citation

Ferraro, D.J.,Okerlund, A.,Brown, E.,Ramaswamy, S.
One enzyme, many reactions: structural basis for the various reactions catalyzed by naphthalene 1,2-dioxygenase.
Iucrj, 4:648-656, 2017

PubMed Abstract: Rieske nonheme iron oxygenases (ROs) are a well studied class of enzymes. Naphthalene 1,2-dioxygenase (NDO) is used as a model to study ROs. Previous work has shown how side-on binding of oxygen to the mononuclear iron provides this enzyme with the ability to catalyze stereospecific and regiospecific -dihydroxylation reactions. It has been well documented that ROs catalyze a variety of other reactions, including mono-oxygenation, desaturation, O- and N-dealkylation, sulfoxidation . NDO itself catalyzes a variety of these reactions. Structures of NDO in complex with a number of different substrates show that the orientation of the substrate in the active site controls not only the regiospecificity and stereospecificity, but also the type of reaction catalyzed. It is proposed that the mononuclear iron-activated dioxygen attacks the atoms of the substrate that are most proximal to it. The promiscuity of delivering two products (apparently by two different reactions) from the same substrate can be explained by the possible binding of the substrate in slightly different orientations aided by the observed flexibility of residues in the binding pocket.

PubMed: 28989720
DOI: 10.1107/S2052252517008223

Experimental method

X-RAY DIFFRACTION (1.5 Å)