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| - | [[Image:1npf.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1npf| PDB=1npf | SCENE= }} | | {{STRUCTURE_1npf| PDB=1npf | SCENE= }} |
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| - | '''MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE'''
| + | ===MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE=== |
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| - | ==Overview==
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| - | The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO-containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of horse heart (hh) MbNO from nitrosylation of aqua-metMb crystals, and we have determined the crystal structure of hh MbNO at a resolution of 1.9 A. The Fe-N-O angle of 147 degrees in hh MbNO is larger than the corresponding 112 degrees angle previously determined from the crystal structure of sperm whale MbNO (Brucker et al., Proteins 1998;30:352-356) but is similar to the 150 degrees angle determined from a MS XAFS study of a frozen solution of hh MbNO (Rich et al., J Am Chem Soc 1998;120:10827-10836). The Fe-N(O) bond length of 2.0 A (this work) is longer than the 1.75 A distance determined from the XAFS study and suggests distal pocket influences on FeNO geometry. The nitrosyl N atom is located 3.0 A from the imidazole N(epsilon) atom of the distal His64 residue, suggesting electrostatic stabilization of the FeNO moiety by His64. The crystal structure of the nitrosoethane adduct of ferrous hh Mb was determined at a resolution of 1.7 A. The nitroso O atom of the EtNO ligand is located 2.7 A from the imidazole N(epsilon) atom of His64, suggesting a hydrogen bond interaction between these groups. To the best of our knowledge, the crystal structure of hh Mb(EtNO) is the first such determination of a nitrosoalkane adduct of a heme protein. | + | The line below this paragraph, {{ABSTRACT_PUBMED_14517970}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14517970 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14517970}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: No]] | | [[Category: No]] |
| | [[Category: Oxygen storage]] | | [[Category: Oxygen storage]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:49:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:13:45 2008'' |
Revision as of 04:13, 28 July 2008
Template:STRUCTURE 1npf
MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE
Template:ABSTRACT PUBMED 14517970
About this Structure
1NPF is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane., Copeland DM, West AH, Richter-Addo GB, Proteins. 2003 Nov 1;53(2):182-92. PMID:14517970
Page seeded by OCA on Mon Jul 28 07:13:45 2008
