1c4c
From Proteopedia
(New page: 200px<br /><applet load="1c4c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c4c, resolution 2.40Å" /> '''BINDING OF EXOGENOUS...) |
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| - | [[Image:1c4c.jpg|left|200px]]<br /><applet load="1c4c" size=" | + | [[Image:1c4c.jpg|left|200px]]<br /><applet load="1c4c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c4c, resolution 2.40Å" /> | caption="1c4c, resolution 2.40Å" /> | ||
'''BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM'''<br /> | '''BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A site for the binding of exogenously added carbon monoxide has been | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1C4C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with HC0, SF4 and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] Full crystallographic information is available from [http:// | + | 1C4C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with <scene name='pdbligand=HC0:'>HC0</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ferredoxin hydrogenase]] | [[Category: Ferredoxin hydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lemon, B | + | [[Category: Lemon, B J.]] |
| - | [[Category: Peters, J | + | [[Category: Peters, J W.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: HC0]] | [[Category: HC0]] | ||
| Line 24: | Line 24: | ||
[[Category: proton reduction]] | [[Category: proton reduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:19 2008'' |
Revision as of 10:02, 21 February 2008
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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.
About this Structure
1C4C is a Single protein structure of sequence from Clostridium pasteurianum with , and as ligands. Active as Ferredoxin hydrogenase, with EC number 1.12.7.2 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[[Category: [fes] clusters]]
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