2z8a: Difference between revisions

Revision as of 03:18, 29 July 2008

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File:2z8a.png

Template:STRUCTURE 2z8a

Ligand Migration and Binding in The Dimeric Hemoglobin of Scapharca Inaequivalvis: I25W with CO Bound to HEME and in the Presence of 3 Atoms of XELigand Migration and Binding in The Dimeric Hemoglobin of Scapharca Inaequivalvis: I25W with CO Bound to HEME and in the Presence of 3 Atoms of XE

Template:ABSTRACT PUBMED 18001141

About this StructureAbout this Structure

2Z8A is a Single protein structure of sequence from Scapharca inaequivalvis. Full crystallographic information is available from OCA.

ReferenceReference

Ligand migration and binding in the dimeric hemoglobin of Scapharca inaequivalvis., Nienhaus K, Knapp JE, Palladino P, Royer WE Jr, Nienhaus GU, Biochemistry. 2007 Dec 11;46(49):14018-31. Epub 2007 Nov 15. PMID:18001141

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

OCA

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-'''Ligand Migration and Binding in The Dimeric Hemoglobin of Scapharca Inaequivalvis: I25W with CO Bound to HEME and in the Presence of 3 Atoms of XE'''
+===Ligand Migration and Binding in The Dimeric Hemoglobin of Scapharca Inaequivalvis: I25W with CO Bound to HEME and in the Presence of 3 Atoms of XE===
-==Overview==
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-Using Fourier transform infrared (FTIR) spectroscopy combined with temperature derivative spectroscopy (TDS) at cryogenic temperatures, we have studied CO binding to the heme and CO migration among cavities in the interior of the dimeric hemoglobin of Scapharca inaequivalvis (HbI) after photodissociation. By combining these studies with X-ray crystallography, three transient ligand docking sites were identified: a primary docking site B in close vicinity to the heme iron, and two secondary docking sites C and D corresponding to the Xe4 and Xe2 cavities of myoglobin. To assess the relevance of these findings for physiological binding, we also performed flash photolysis experiments on HbICO at room temperature and equilibrium binding studies with dioxygen. Our results show that the Xe4 and Xe2 cavities serve as transient docking sites for unbound ligands in the protein, but not as way stations on the entry/exit pathway. For HbI, the so-called histidine gate mechanism proposed for other globins appears as a plausible entry/exit route as well.
+The line below this paragraph, {{ABSTRACT_PUBMED_18001141}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Oxygen storage/transport]]
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