1UUW
NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.
1UUW の概要
| エントリーDOI | 10.2210/pdb1uuw/pdb |
| 関連するPDBエントリー | 1EG9 1NDO 1O7G 1O7H 1O7M 1O7N 1O7P 1O7W 1UUV |
| 分子名称 | NAPHTHALENE 1,2-DIOXYGENASE ALPHA SUBUNIT, NAPHTHALENE 1,2-DIOXYGENASE BETA SUBUNIT, FE2/S2 (INORGANIC) CLUSTER, ... (7 entities in total) |
| 機能のキーワード | oxidoreductase, non-heme iron dioxygenase, enzyme-substrate complex, aromatic hydrocarbons catabolism, metal-binding, iron-sulfur, iron, 2fe-2s, dioxygenase, nad, plasmid |
| 由来する生物種 | PSEUDOMONAS PUTIDA 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 73087.24 |
| 構造登録者 | Karlsson, A.,Parales, J.V.,Parales, R.E.,Gibson, D.T.,Eklund, H.,Ramaswamy, S. (登録日: 2004-01-11, 公開日: 2005-02-09, 最終更新日: 2023-12-13) |
| 主引用文献 | 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 Cited by 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: 15942729DOI: 10.1007/S00775-005-0657-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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