2e7e
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cyanide is a well known potent inhibitor of haem proteins, including haem | + | Cyanide is a well known potent inhibitor of haem proteins, including haem oxygenase (HO). Generally, cyanide coordinates to the ferric haem iron with a linear binding geometry; the Fe-C-N angle ranges from 160 to 180 degrees . The Fe-C-N angle observed in the crystal structure of haem-HO bound to cyanide prepared at alkaline pH was 166 degrees . Here, it is reported that cyanide can bind to the haem iron in HO in a bent mode when the ternary complex is prepared at neutral pH; a crystal structure showed that the Fe-C-N angle was bent by 47 degrees . Unlike the ternary complex prepared at alkaline pH, in which the haem group, including the proximal ligand and the distal helix, was displaced upon cyanide binding, the positions of the haem group and the distal helix in the complex prepared at neutral pH were nearly identical to those in haem-HO. Cyanide that was bound to haem-HO with a bent geometry was readily photodissociated, whereas that bound with a linear geometry was not photodissociated. Thus, alternative cyanide-binding modes with linear and bent geometries exist in the crystalline state of haem-HO. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Alternative cyanide-binding modes to the haem iron in haem oxygenase., Sugishima M, Oda K, Ogura T, Sakamoto H, Noguchi M, Fukuyama K, Acta | + | Alternative cyanide-binding modes to the haem iron in haem oxygenase., Sugishima M, Oda K, Ogura T, Sakamoto H, Noguchi M, Fukuyama K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):471-4. Epub 2007 May 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17554165 17554165] |
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: ligand]] | [[Category: ligand]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:51 2008'' |
Revision as of 15:06, 21 February 2008
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Bent-binding of cyanide to the heme iron in rat heme oxygenase-1
Overview
Cyanide is a well known potent inhibitor of haem proteins, including haem oxygenase (HO). Generally, cyanide coordinates to the ferric haem iron with a linear binding geometry; the Fe-C-N angle ranges from 160 to 180 degrees . The Fe-C-N angle observed in the crystal structure of haem-HO bound to cyanide prepared at alkaline pH was 166 degrees . Here, it is reported that cyanide can bind to the haem iron in HO in a bent mode when the ternary complex is prepared at neutral pH; a crystal structure showed that the Fe-C-N angle was bent by 47 degrees . Unlike the ternary complex prepared at alkaline pH, in which the haem group, including the proximal ligand and the distal helix, was displaced upon cyanide binding, the positions of the haem group and the distal helix in the complex prepared at neutral pH were nearly identical to those in haem-HO. Cyanide that was bound to haem-HO with a bent geometry was readily photodissociated, whereas that bound with a linear geometry was not photodissociated. Thus, alternative cyanide-binding modes with linear and bent geometries exist in the crystalline state of haem-HO.
About this Structure
2E7E is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as Heme oxygenase, with EC number 1.14.99.3 Full crystallographic information is available from OCA.
Reference
Alternative cyanide-binding modes to the haem iron in haem oxygenase., Sugishima M, Oda K, Ogura T, Sakamoto H, Noguchi M, Fukuyama K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):471-4. Epub 2007 May 31. PMID:17554165
Page seeded by OCA on Thu Feb 21 17:06:51 2008
Categories: Heme oxygenase | Rattus norvegicus | Single protein | Fukuyama, K. | Sugishima, M. | CYN | HEM | Binding geometry | Heme | Ligand
