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  Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase - structural models of the short-lived oxygen complexes

Fedorov, R., Ghosh, D. K., & Schlichting, I. (2003). Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase - structural models of the short-lived oxygen complexes. Archives of Biochemistry and Biophysics, 409(1): 1, pp. 25-31. Retrieved from http://dx.doi.org/10.1016/S0003-9861(02)00555-6.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-0CB8-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-0CB9-D
Genre: Journal Article
Alternative Title : Arch. Biochem. Biophys.

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 Creators:
Fedorov, Roman1, Author
Ghosh, Dipak K., Author
Schlichting, Ilme2, Author              
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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Free keywords: hemoprotein; oxygen analogue; crystal structure; nitric oxide synthase; CYP; monooxygenase; oxygen; X-ray radiolysis; reaction mechanism
 Abstract: The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8 Angstrom 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, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4 Angstrom resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8 Angstrom 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. (C) 2002 Elsevier Science (USA). All rights reserved.

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Language(s): eng - English
 Dates: 2003-01-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Archives of Biochemistry and Biophysics
  Alternative Title : Arch. Biochem. Biophys.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 409 (1) Sequence Number: 1 Start / End Page: 25 - 31 Identifier: -