2fc1: Difference between revisions

Revision as of 06:52, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fc1.png

Template:STRUCTURE 2fc1

Heme NO Complex in NOSHeme NO Complex in NOS

Template:ABSTRACT PUBMED 16489746

About this StructureAbout this Structure

2FC1 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation., Pant K, Crane BR, Biochemistry. 2006 Feb 28;45(8):2537-44. PMID:16489746

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OCA

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-'''Heme NO Complex in NOS'''
+===Heme NO Complex in NOS===
-==Overview==
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-The crystal structures of nitrosyl-heme complexes of a prokaryotic nitric oxide synthase (NOS) from Bacillus subtilis (bsNOS) reveal changes in active-site hydrogen bonding in the presence of the intermediate N(omega)-hydroxy-l-arginine (NOHA) compared to the substrate l-arginine (l-Arg). Correlating with a Val-to-Ile residue substitution in the bsNOS heme pocket, the Fe(II)-NO complex with both l-Arg and NOHA is more bent than the Fe(II)-NO, l-Arg complex of mammalian eNOS [Li, H., Raman, C. S., Martasek, P., Masters, B. S. S., and Poulos, T. L. (2001) Biochemistry 40, 5399-5406]. Structures of the Fe(III)-NO complex with NOHA show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound NOHA. In the Fe(II)-NO complexes, the protonated NOHA N(omega) atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. In contrast, the l-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen. This difference in hydrogen bonding to the nitrosyl group by the two substrates indicates that interactions provided by NOHA may preferentially stabilize an electrophilic peroxo-heme intermediate in the second step of NOS catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_16489746}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16489746 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16489746}}
 ==About this Structure==
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 [[Category: Heme-no complex]]
 [[Category: Nitric oxide synthase]]
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