1ebc
From Proteopedia
(New page: 200px<br /> <applet load="1ebc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ebc, resolution 1.8Å" /> '''SPERM WHALE MET-MYOG...) |
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| - | [[Image:1ebc.gif|left|200px]]<br /> | + | [[Image:1ebc.gif|left|200px]]<br /><applet load="1ebc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ebc" size=" | + | |
caption="1ebc, resolution 1.8Å" /> | caption="1ebc, resolution 1.8Å" /> | ||
'''SPERM WHALE MET-MYOGLOBIN:CYANIDE COMPLEX'''<br /> | '''SPERM WHALE MET-MYOGLOBIN:CYANIDE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The x-ray crystal structures of the cyanide derivative of Lucina pectinata | + | The x-ray crystal structures of the cyanide derivative of Lucina pectinata monomeric hemoglobin I (L. pectinata HbI) and sperm whale (Physeter catodon) myoglobin (Mb), generally taken as reference models for monomeric hemoproteins carrying hydrogen sulfide and oxygen, respectively, have been determined at 1.9 A (R-factor = 0. 184), and 1.8 A (R-factor = 0.181) resolution, respectively, at room temperature (lambda = 1.542 A). Moreover, the x-ray crystal structure of the L. pectinata HbI:cyanide derivative has been studied at 1.4-A resolution (R-factor = 0.118) and 100 K (on a synchrotron source lambda = 0.998 A). At room temperature, the cyanide ligand is roughly parallel to the heme plane of L. pectinata HbI, being located approximately 2.5 A from the iron atom. On the other hand, the crystal structure of the L. pectinata HbI:cyanide derivative at 100 K shows that the diatomic ligand is coordinated to the iron atom in an orientation almost perpendicular to the heme (the Fe-C distance being 1.95 A), adopting a coordination geometry strictly reminescent of that observed in sperm whale Mb, at room temperature. The unusual cyanide distal site orientation observed in L. pectinata HbI, at room temperature, may reflect reduction of the heme Fe(III) atom induced by free radical species during x-ray data collection using Cu Kalpha radiation. |
==About this Structure== | ==About this Structure== | ||
| - | 1EBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with CYN, SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1EBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=CYN:'>CYN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxigen storage]] | [[Category: oxigen storage]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:58 2008'' |
Revision as of 10:25, 21 February 2008
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SPERM WHALE MET-MYOGLOBIN:CYANIDE COMPLEX
Overview
The x-ray crystal structures of the cyanide derivative of Lucina pectinata monomeric hemoglobin I (L. pectinata HbI) and sperm whale (Physeter catodon) myoglobin (Mb), generally taken as reference models for monomeric hemoproteins carrying hydrogen sulfide and oxygen, respectively, have been determined at 1.9 A (R-factor = 0. 184), and 1.8 A (R-factor = 0.181) resolution, respectively, at room temperature (lambda = 1.542 A). Moreover, the x-ray crystal structure of the L. pectinata HbI:cyanide derivative has been studied at 1.4-A resolution (R-factor = 0.118) and 100 K (on a synchrotron source lambda = 0.998 A). At room temperature, the cyanide ligand is roughly parallel to the heme plane of L. pectinata HbI, being located approximately 2.5 A from the iron atom. On the other hand, the crystal structure of the L. pectinata HbI:cyanide derivative at 100 K shows that the diatomic ligand is coordinated to the iron atom in an orientation almost perpendicular to the heme (the Fe-C distance being 1.95 A), adopting a coordination geometry strictly reminescent of that observed in sperm whale Mb, at room temperature. The unusual cyanide distal site orientation observed in L. pectinata HbI, at room temperature, may reflect reduction of the heme Fe(III) atom induced by free radical species during x-ray data collection using Cu Kalpha radiation.
About this Structure
1EBC is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
Reference
Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study., Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P, Biophys J. 1999 Aug;77(2):1093-9. PMID:10423453
Page seeded by OCA on Thu Feb 21 12:25:58 2008
Categories: Physeter catodon | Single protein | Ascenzi, P. | Bolognesi, M. | Losso, R. | Rizzi, M. | Rosano, C. | CYN | HEM | SO4 | Globins | Hemoprotein | Oxigen storage
