The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron
Abstract
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
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Self-citationCrystal structure of substrate-free Pseudomonas putida cytochrome P-450
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Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase
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Sugimoto, H., Oda, S.-I., Otsuki, T., Hino, T., Yoshida, T., & Shiro, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508996103 · Cited by 441
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Zhu, Y., Jameson, E., Crosatti, M., Schäfer, H., Rajakumar, K., Bugg, T. D. H., & Chen, Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316569111 · Cited by 372
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Metadata
- Authors
- Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., & Ramaswamy, S.
- Venue
- Science
- Published
- 2003-02-14
- Volume
- 299
- Issue
- 5609
- Pages
- 1039-1042
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2020100815
- Cited by
- 560
- References
- 18
- FWCI
- 34.74
- Type
- journal article
- Language
- en
- Open access
- closed
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