This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1c4c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1c4c.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1c4c.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1c4c| PDB=1c4c | SCENE= }}
{{STRUCTURE_1c4c| PDB=1c4c | SCENE= }}
-
'''BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM'''
+
===BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM===
-
==Overview==
+
<!--
-
A site for the binding of exogenously added carbon monoxide has been identified at the active site of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum. The binding and inhibition of carbon monoxide have been exploited in biochemical and spectroscopic studies to gain mechanistic insights. In the present study, we have taken advantage of the ability to generate an irreversibly carbon monoxide bound state of CpI. The crystallization and structural characterization of CpI inhibited in the presence of carbon monoxide indicates the addition of a single molecule of carbon monoxide. The ability to generate crystals of the carbon monoxide bound state of the hydrogenase that are isomorphous to those of the native enzyme has allowed for a direct comparison of the crystallographic data and an unambiguous identification of the site of carbon monoxide binding at the active site of CpI. Carbon monoxide binds to an Fe atom of the 2Fe subcluster at the site of a terminally bound water molecule in the as crystallized native state of CpI that has been previously suggested to be a potential site of reversible hydrogen oxidation. Binding of carbon monoxide at this site results in an active site that is coordinately saturated with strong ligands (S, CO, and CN), providing a rational potential mechanism for inhibition of reversible hydrogen oxidation at the active site of CpI.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10529166}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10529166 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10529166}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
[[Category: Proton reduction]]
[[Category: Proton reduction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:18:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:11:35 2008''

Revision as of 17:11, 30 June 2008

Image:1c4c.png

Template:STRUCTURE 1c4c

BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM

Template:ABSTRACT PUBMED 10529166

About this Structure

1C4C is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.

Reference

Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum., Lemon BJ, Peters JW, Biochemistry. 1999 Oct 5;38(40):12969-73. PMID:10529166

Page seeded by OCA on Mon Jun 30 20:11:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c4c"
Personal tools