1uuw: Difference between revisions

Revision as of 22:25, 27 July 2008

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File:1uuw.png

Template:STRUCTURE 1uuw

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

Template:ABSTRACT PUBMED 15942729

About this StructureAbout this Structure

1UUW is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

NO binding to naphthalene dioxygenase., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, J Biol Inorg Chem. 2005 Aug;10(5):483-9. Epub 2005 Sep 23. PMID:15942729

Page seeded by OCA on Sun Jul 27 22:25:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.'''
+===NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15942729}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15942729 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15942729}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Plasmid]]
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