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| | ==Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form with ascorbate - partly reduced state== | | ==Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form with ascorbate - partly reduced state== |
| - | <StructureSection load='4iud' size='340' side='right' caption='[[4iud]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='4iud' size='340' side='right'caption='[[4iud]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4iud]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_eutropha_h16 Alcaligenes eutropha h16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IUD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4iud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IUD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFV:NI-FE+OXIDIZED+ACTIVE+CENTER'>NFV</scene>, <scene name='pdbligand=S3F:OXIDIZED+[FE4-S3]+CLUSTER'>S3F</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFV:NI-FE+OXIDIZED+ACTIVE+CENTER'>NFV</scene>, <scene name='pdbligand=S3F:OXIDIZED+[FE4-S3]+CLUSTER'>S3F</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iub|4iub]], [[4iuc|4iuc]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4iud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iud OCA], [https://pdbe.org/4iud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iud RCSB], [https://www.ebi.ac.uk/pdbsum/4iud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iud ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hoxG, PHG002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381666 Alcaligenes eutropha H16]), hoxK, PHG001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381666 Alcaligenes eutropha H16])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen:quinone_oxidoreductase Hydrogen:quinone oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.5.1 1.12.5.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iud OCA], [http://pdbe.org/4iud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iud RCSB], [http://www.ebi.ac.uk/pdbsum/4iud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iud ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MBHL_CUPNH MBHL_CUPNH]] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. [[http://www.uniprot.org/uniprot/MBHS_CUPNH MBHS_CUPNH]] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. | + | [https://www.uniprot.org/uniprot/MBHL_CUPNH MBHL_CUPNH] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcaligenes eutropha h16]] | + | [[Category: Cupriavidus necator H16]] |
| - | [[Category: Hydrogen:quinone oxidoreductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Frielingsdorf, S]] | + | [[Category: Frielingsdorf S]] |
| - | [[Category: Fritsch, J]] | + | [[Category: Fritsch J]] |
| - | [[Category: Hammer, M]] | + | [[Category: Hammer M]] |
| - | [[Category: Lenz, O]] | + | [[Category: Lenz O]] |
| - | [[Category: Scheerer, P]] | + | [[Category: Scheerer P]] |
| - | [[Category: Schmidt, A]] | + | [[Category: Schmidt A]] |
| - | [[Category: Aerobic hydrogen bacteria]]
| + | |
| - | [[Category: Bimetallic]]
| + | |
| - | [[Category: Hydrogen catalysis]]
| + | |
| - | [[Category: Iron-sulfur cluster]]
| + | |
| - | [[Category: Knallgas bacteria]]
| + | |
| - | [[Category: Membrane-bound]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| - | [[Category: Metalloprotein catalytic center]]
| + | |
| - | [[Category: Ni-fe active site]]
| + | |
| - | [[Category: Nickel-iron cofactor]]
| + | |
| - | [[Category: Oxidized state]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen-tolerant hydrogenase]]
| + | |
| - | [[Category: Proteobacteria]]
| + | |
| - | [[Category: Reduced state]]
| + | |
| Structural highlights
4iud is a 2 chain structure with sequence from Cupriavidus necator H16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.45Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MBHL_CUPNH This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Publication Abstract from PubMed
Hydrogenases catalyze the reversible oxidation of H2 into protons and electrons and are usually readily inactivated by O2. However, a subgroup of the [NiFe] hydrogenases, including the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha, has evolved remarkable tolerance toward O2 that enables their host organisms to utilize H2 as an energy source at high O2. This feature is crucially based on a unique six cysteine-coordinated [4Fe-3S] cluster located close to the catalytic center, whose properties were investigated in this study using a multidisciplinary approach. The [4Fe-3S] cluster undergoes redox-dependent reversible transformations, namely iron swapping between a sulfide and a peptide amide N. Moreover, our investigations unraveled the redox-dependent and reversible occurence of an oxygen ligand located at a different iron. This ligand is hydrogen bonded to a conserved histidine that is essential for H2 oxidation at high O2. We propose that these transformations, reminiscent of those of the P-cluster of nitrogenase, enable the consecutive transfer of two electrons within a physiological potential range.
Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase.,Frielingsdorf S, Fritsch J, Schmidt A, Hammer M, Lowenstein J, Siebert E, Pelmenschikov V, Jaenicke T, Kalms J, Rippers Y, Lendzian F, Zebger I, Teutloff C, Kaupp M, Bittl R, Hildebrandt P, Friedrich B, Lenz O, Scheerer P Nat Chem Biol. 2014 May;10(5):378-85. doi: 10.1038/nchembio.1500. Epub 2014 Apr, 6. PMID:24705592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Frielingsdorf S, Fritsch J, Schmidt A, Hammer M, Lowenstein J, Siebert E, Pelmenschikov V, Jaenicke T, Kalms J, Rippers Y, Lendzian F, Zebger I, Teutloff C, Kaupp M, Bittl R, Hildebrandt P, Friedrich B, Lenz O, Scheerer P. Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase. Nat Chem Biol. 2014 May;10(5):378-85. doi: 10.1038/nchembio.1500. Epub 2014 Apr, 6. PMID:24705592 doi:http://dx.doi.org/10.1038/nchembio.1500
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