1yrq
From Proteopedia
(New page: 200px<br /><applet load="1yrq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yrq, resolution 2.10Å" /> '''Structure of the rea...) |
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| - | [[Image:1yrq.gif|left|200px]]<br /><applet load="1yrq" size=" | + | [[Image:1yrq.gif|left|200px]]<br /><applet load="1yrq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yrq, resolution 2.10Å" /> | caption="1yrq, resolution 2.10Å" /> | ||
'''Structure of the ready oxidized form of [NiFe]-hydrogenase'''<br /> | '''Structure of the ready oxidized form of [NiFe]-hydrogenase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | [NiFe] hydrogenases catalyze the reversible heterolytic cleavage of | + | [NiFe] hydrogenases catalyze the reversible heterolytic cleavage of molecular hydrogen. Several oxidized, inactive states of these enzymes are known that are distinguishable by their very different activation properties. So far, the structural basis for this difference has not been understood because of lack of relevant crystallographic data. Here, we present the crystal structure of the ready Ni-B state of Desulfovibrio fructosovorans [NiFe] hydrogenase and show it to have a putative mu-hydroxo Ni-Fe bridging ligand at the active site. On the other hand, a new, improved refinement procedure of the X-ray diffraction data obtained for putative unready Ni-A/Ni-SU states resulted in a more elongated electron density for the bridging ligand, suggesting that it is a diatomic species. The slow activation of the Ni-A state, compared with the rapid activation of the Ni-B state, is therefore proposed to result from the different chemical nature of the ligands in the two oxidized species. Our results along with very recent electrochemical studies suggest that the diatomic ligand could be hydro-peroxide. |
==About this Structure== | ==About this Structure== | ||
| - | 1YRQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_fructosovorans Desulfovibrio fructosovorans] with NI, MG, SF4, F3S and FCO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c3_hydrogenase Cytochrome-c3 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.2.1 1.12.2.1] Full crystallographic information is available from [http:// | + | 1YRQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_fructosovorans Desulfovibrio fructosovorans] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=F3S:'>F3S</scene> and <scene name='pdbligand=FCO:'>FCO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c3_hydrogenase Cytochrome-c3 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.2.1 1.12.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Desulfovibrio fructosovorans]] | [[Category: Desulfovibrio fructosovorans]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Albracht, S | + | [[Category: Albracht, S P.]] |
[[Category: Cavazza, C.]] | [[Category: Cavazza, C.]] | ||
| - | [[Category: Faber, B | + | [[Category: Faber, B W.]] |
| - | [[Category: Fontecilla-Camps, J | + | [[Category: Fontecilla-Camps, J C.]] |
[[Category: Garcin, E.]] | [[Category: Garcin, E.]] | ||
[[Category: Martin, L.]] | [[Category: Martin, L.]] | ||
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[[Category: nib state]] | [[Category: nib state]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:23 2008'' |
Revision as of 14:08, 21 February 2008
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Structure of the ready oxidized form of [NiFe]-hydrogenase
Overview
[NiFe] hydrogenases catalyze the reversible heterolytic cleavage of molecular hydrogen. Several oxidized, inactive states of these enzymes are known that are distinguishable by their very different activation properties. So far, the structural basis for this difference has not been understood because of lack of relevant crystallographic data. Here, we present the crystal structure of the ready Ni-B state of Desulfovibrio fructosovorans [NiFe] hydrogenase and show it to have a putative mu-hydroxo Ni-Fe bridging ligand at the active site. On the other hand, a new, improved refinement procedure of the X-ray diffraction data obtained for putative unready Ni-A/Ni-SU states resulted in a more elongated electron density for the bridging ligand, suggesting that it is a diatomic species. The slow activation of the Ni-A state, compared with the rapid activation of the Ni-B state, is therefore proposed to result from the different chemical nature of the ligands in the two oxidized species. Our results along with very recent electrochemical studies suggest that the diatomic ligand could be hydro-peroxide.
About this Structure
1YRQ is a Protein complex structure of sequences from Desulfovibrio fructosovorans with , , , and as ligands. Active as Cytochrome-c3 hydrogenase, with EC number 1.12.2.1 Full crystallographic information is available from OCA.
Reference
Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases., Volbeda A, Martin L, Cavazza C, Matho M, Faber BW, Roseboom W, Albracht SP, Garcin E, Rousset M, Fontecilla-Camps JC, J Biol Inorg Chem. 2005 May;10(3):239-49. Epub 2005 Apr 1. PMID:15803334
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