7AIZ
Vanadium nitrogenase VFe protein, high CO state
Summary for 7AIZ
| Entry DOI | 10.2210/pdb7aiz/pdb |
| Related | 7ADR |
| Descriptor | Nitrogenase vanadium-iron protein alpha chain, FE(8)-S(7) CLUSTER, MAGNESIUM ION, ... (12 entities in total) |
| Functional Keywords | nitrogenase, nitrogen fixation, co reduction, atomic resolution, oxidoreductase |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 6 |
| Total formula weight | 244877.82 |
| Authors | Rohde, M.,Einsle, O. (deposition date: 2020-09-28, release date: 2021-06-09, Last modification date: 2024-01-31) |
| Primary citation | Rohde, M.,Laun, K.,Zebger, I.,Stripp, S.T.,Einsle, O. Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (CH), implying a C-C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion. PubMed: 34049880DOI: 10.1126/sciadv.abg4474 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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