NDLI: Alternative cyanide-binding modes to the haem iron in haem oxygenase.

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Alternative cyanide-binding modes to the haem iron in haem oxygenase.

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Alternative cyanide-binding modes to the haem iron in haem oxygenase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sugishima, Masakazu Oda, Kenji Ogura, Takashi Sakamoto, Hiroshi Noguchi, Masato Fukuyama, Keiichi
Description	Country affiliation: Japan Author Affiliation: Sugishima M ( Department of Medical Biochemistry, Kurume University School of Medicine, Japan.)
Abstract	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.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 6
Volume Number	63
Language	English
Publisher	Wiley
Publisher Date	2007-06-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Cyanides Metabolism Heme Oxygenase (decyclizing) Heme Animals Binding Sites Physiology Crystallography, X-ray Chemistry Comparative Study Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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