Sandbox Reserved 496: Difference between revisions

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Five of the metalloclusters (two B-, two C-, and one D-cluster) are located in the β2 portion of the protein with a B- and C-cluster in each β subunit and the sole D-cluster bridging the two subunits. The B- and D-clusters consist of [Fe4S4] centers that serve to transfer electrons. As the active site in each β subunit where CODH activity occurs, the C-clusters are composed of a Fe -[NiFe3S4] cage with the unique Fe coordinated by a bridging sulfur ion, His283, and Cys317 <ref name="Zn">PMID:12627225</ref>. The B- and D-clusters are positioned in relation to the α-helical domain of the β subunit, while the C-clusters are aligned through interactions with both Rossmann-like domains <ref name="Xe"/>. A ligand binding study with the native CODH/ACS structure and with cyanide used as competitive inhibitor for CO showed that H2O/OH- binds the C-cluster at the unique Fe and CO binds the C-cluster at the Ni ion <ref name="CN"/>.

<scene name='Sandbox_Reserved_496/Beta_metalloclusters/1'>Five of the metalloclusters</scene> ('''two B-''', '''two C-''', and '''one D-cluster''') are located in the β2 portion of the protein with a B- and C-cluster in each β subunit and the sole D-cluster bridging the two subunits. The B- and D-clusters consist of [Fe4S4] centers that serve to transfer electrons. As the active site in each β subunit where CODH activity occurs, the C-clusters are composed of a Fe -[NiFe3S4] cage with the unique Fe coordinated by a bridging sulfur ion, His283, and Cys317 <ref name="Zn">PMID:12627225</ref>. The B- and D-clusters are positioned in relation to the α-helical domain of the β subunit, while the C-clusters are aligned through interactions with both Rossmann-like domains <ref name="Xe"/>. A ligand binding study with the native CODH/ACS structure and with cyanide used as competitive inhibitor for CO showed that H2O/OH- binds the C-cluster at the unique Fe and CO binds the C-cluster at the Ni ion <ref name="CN"/>.

Sandbox Reserved 496: Difference between revisions

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Revision as of 22:08, 2 May 2012 view source Rachel Slivka (talk \| contribs) 49 edits No edit summary ← Older edit		Revision as of 22:39, 2 May 2012 view source Rachel Slivka (talk \| contribs) 49 edits No edit summary Newer edit →
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	Five of the metalloclusters (two B-, two C-, and one D-cluster) are located in the β2 portion of the protein with a B- and C-cluster in each β subunit and the sole D-cluster bridging the two subunits. The B- and D-clusters consist of [Fe4S4] centers that serve to transfer electrons. As the active site in each β subunit where CODH activity occurs, the C-clusters are composed of a Fe -[NiFe3S4] cage with the unique Fe coordinated by a bridging sulfur ion, His283, and Cys317 <ref name="Zn">PMID:12627225</ref>. The B- and D-clusters are positioned in relation to the α-helical domain of the β subunit, while the C-clusters are aligned through interactions with both Rossmann-like domains <ref name="Xe"/>. A ligand binding study with the native CODH/ACS structure and with cyanide used as competitive inhibitor for CO showed that H2O/OH- binds the C-cluster at the unique Fe and CO binds the C-cluster at the Ni ion <ref name="CN"/>.		<scene name='Sandbox_Reserved_496/Beta_metalloclusters/1'>Five of the metalloclusters</scene> (<font color='red'>'''two B-'''</font>, <font color='blue'>'''two C-'''</font>, and <font color='green'>'''one D-cluster'''</font>) are located in the β2 portion of the protein with a B- and C-cluster in each β subunit and the sole D-cluster bridging the two subunits. The B- and D-clusters consist of [Fe4S4] centers that serve to transfer electrons. As the active site in each β subunit where CODH activity occurs, the C-clusters are composed of a Fe -[NiFe3S4] cage with the unique Fe coordinated by a bridging sulfur ion, His283, and Cys317 <ref name="Zn">PMID:12627225</ref>. The B- and D-clusters are positioned in relation to the α-helical domain of the β subunit, while the C-clusters are aligned through interactions with both Rossmann-like domains <ref name="Xe"/>. A ligand binding study with the native CODH/ACS structure and with cyanide used as competitive inhibitor for CO showed that H2O/OH- binds the C-cluster at the unique Fe and CO binds the C-cluster at the Ni ion <ref name="CN"/>.