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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biomolekulare Mechanismen     Display Documents

ID: 23029.0, MPI für medizinische Forschung / Abteilung Biomolekulare Mechanismen
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase--structural models of the short-lived oxygen complexes
Authors:Fedorov, Roman; Ghosh, Dipak K.; Schlichting, Ilme
Date of Publication (YYYY-MM-DD):2003-01-01
Title of Journal:Archives of Biochemistry and Biophysics
Journal Abbrev.:Arch. Biochem. Biophys.
Issue / Number:1
Start Page:25
End Page:31
Copyright:Copyright © 2002 Elsevier Science (USA). All rights reserved.
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8 Å resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, Image-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4 Å resolution. Cyanide binds essentially linearly, interacts with Image-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8 Å from the nitrogen atom of cyanide, and could provide a proton required for O–O bond scission in the hydroxylation reaction of nitric oxide synthase.
Free Keywords:Hemoprotein; Oxygen analogue; Crystal structure; Nitric oxide synthase; CYP; Monooxygenase; Oxygen; X-ray radiolysis; Reaction mechanism
Comment of the Author/Creator:We are grateful to Stephen G. Sligar for providing the P450cam clone and to Christiane Jung for helpful suggestions concerning protein expression and purification. We thank Elisabeth Hartmann and Georg Holtermann for excellent technical assistance; Kelvin Chu and the staff at the ESRF, Grenoble, France, for help during data collection; Robert M. Sweet and Roger S. Goody for continuous encouragement and support. D.K.G. is very grateful to Dr. J.B. Weinberg for continuing support and for sharing laboratory space for this study.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
External Affiliations:Abt. Biophysikalische Chemie, Max Planck Institut für Molekulare Physiologie, Otto Hahn Strasse 11, 44227, Dortmund, Germany; Duke University and VA Medical Center, Durham, NC 27713, USA
Identifiers:URI:http://www.sciencedirect.com/science?_ob=ArticleUR... [Fulltext HTML]
URI:http://www.sciencedirect.com/science?_ob=ArticleUR... [Abstract HTML]
URI:http://www.sciencedirect.com/science?_ob=MImg&_ima... [Fulltext PDF]
LOCALID:5993 [PUMA publication management ID]
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