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-Structure paper
Title | The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. |
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Journal, issue, pages | Febs Lett., Vol. 583, Page 585-590, Year 2009 |
Publish date | Oct 31, 2008 (structure data deposition date) |
Authors | Hiromoto, T. / Ataka, K. / Pilak, O. / Vogt, S. / Stagni, M.S. / Meyer-Klaucke, W. / Warkentin, E. / Thauer, R.K. / Shima, S. / Ermler, U. |
External links | Febs Lett. / PubMed:19162018 |
Methods | X-ray diffraction |
Resolution | 1.75 - 1.95 Å |
Structure data | PDB-3f46: PDB-3f47: |
Chemicals | ChemComp-I2C: ChemComp-FE2: ChemComp-CMO: ChemComp-DTV: ChemComp-HOH: ChemComp-NA: |
Source |
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Keywords | OXIDOREDUCTASE / ROSSMANN FOLD / HELIX BUNDLE / COMPLEX WITH IRON GUANYLYL PYRIDINOL COFACTOR / C176A MUTANT / Methanogenesis / One-carbon metabolism |