1UUW

NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.

Summary for 1UUW

• Entry DOI: 10.2210/pdb1uuw/pdb
• Related: 1EG9 1NDO 1O7G 1O7H 1O7M 1O7N 1O7P 1O7W 1UUV
• Descriptor: NAPHTHALENE 1,2-DIOXYGENASE ALPHA SUBUNIT, NAPHTHALENE 1,2-DIOXYGENASE BETA SUBUNIT, FE2/S2 (INORGANIC) CLUSTER, ... (7 entities in total)
• Functional Keywords: oxidoreductase, non-heme iron dioxygenase, enzyme-substrate complex, aromatic hydrocarbons catabolism, metal-binding, iron-sulfur, iron, 2fe-2s, dioxygenase, nad, plasmid
• Biological source: PSEUDOMONAS PUTIDA; More
• Total number of polymer chains: 2
• Total formula weight: 73087.24

Authors

Karlsson, A.,Parales, J.V.,Parales, R.E.,Gibson, D.T.,Eklund, H.,Ramaswamy, S. (deposition date: 2004-01-11, release date: 2005-02-09, Last modification date: 2023-12-13)

Primary citation

Karlsson, A.,Parales, J.V.,Parales, R.E.,Gibson, D.T.,Eklund, H.,Ramaswamy, S.
No Binding to Naphthalene Dioxygenase.
J.Biol.Inorg.Chem., 10:483-, 2005

PubMed Abstract: Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation. In this study, crystallographic structures of naphthalene dioxygenase (NDO) in complex with nitric oxide are reported. In the presence of the aromatic substrate indole, NO is bound end-on to the active-site mononuclear iron of NDO. The structural observations correlate well with spectroscopic measurements of NO binding to NDO in solution. However, the end-on binding of NO is in contrast to the recently reported structure of oxygen to the active-site iron of NDO that binds side-on. While NO is a good oxygen analogue with many similarities to O(2), the different binding mode of NO to the active-site iron atom leads to different mechanistic implications. Hence, caution needs to be used in extrapolating NO as an analogue to O(2) binding.

PubMed: 15942729
DOI: 10.1007/S00775-005-0657-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)