Journal:JBIC:31
From Proteopedia
(Difference between revisions)
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* <scene name='69/696899/Cv/5'>Proximal NO complex of SFCP (monomer A)</scene>. | * <scene name='69/696899/Cv/5'>Proximal NO complex of SFCP (monomer A)</scene>. | ||
* <scene name='69/696899/Cv/8'>Click here to see the difference between these structures</scene>. | * <scene name='69/696899/Cv/8'>Click here to see the difference between these structures</scene>. | ||
| - | SFCP exhibits biphasic binding kinetics for both NO and CO as a result of the high level of steric hindrance from the aromatic side chain of residue Phe 16. The binding of distal ligands is thus controlled by the conformation of the phenylalanine ring. Only a proximal 5-coordinate NO adduct, confirmed by structural data, is observed with no detectable hexacoordinate distal NO adduct. | + | SFCP exhibits biphasic binding kinetics for both NO and CO as a result of the high level of steric hindrance from the aromatic side chain of residue Phe 16. The binding of distal ligands is thus controlled by the conformation of the phenylalanine ring. |
| + | * <scene name='69/696899/Cv/12'>A superposition of the heme environments</scene> | ||
| + | |||
| + | Only a proximal 5-coordinate NO adduct, confirmed by structural data, is observed with no detectable hexacoordinate distal NO adduct. | ||
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 11:27, 26 April 2015
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- ↑ Manole A, Kekilli D, Svistunenko DA, Wilson MT, Dobbin PS, Hough MA. Conformational control of the binding of diatomic gases to cytochrome c'. J Biol Inorg Chem. 2015 Mar 20. PMID:25792378 doi:http://dx.doi.org/10.1007/s00775-015-1253-7
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