3LR7
Ferric horse heart myoglobin, nitrite adduct
Summary for 3LR7
| Entry DOI | 10.2210/pdb3lr7/pdb |
| Related | 2frf 3LR9 |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, NITRITE ION, ... (5 entities in total) |
| Functional Keywords | myoglobin, heme, nitrite, metal-binding, muscle protein, oxygen transport, transport |
| Biological source | Equus caballus (domestic horse,equine) |
| Total number of polymer chains | 1 |
| Total formula weight | 17930.14 |
| Authors | Yi, J.,Richter-Addo, G.B. (deposition date: 2010-02-10, release date: 2010-07-07, Last modification date: 2023-09-06) |
| Primary citation | Yi, J.,Orville, A.M.,Skinner, J.M.,Skinner, M.J.,Richter-Addo, G.B. Synchrotron X-ray-Induced Photoreduction of Ferric Myoglobin Nitrite Crystals Gives the Ferrous Derivative with Retention of the O-Bonded Nitrite Ligand. Biochemistry, 49:5969-5971, 2010 Cited by PubMed Abstract: Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. We employed correlated single-crystal spectroscopy with crystallography to further characterize this photoproduct. The 1.55 A resolution crystal structure of the photoproduct reveals retention of the O-binding mode for binding of nitrite to the iron center. The data are consistent with cryogenic generation and trapping, at 100 K, of a ferrous d(6) Mb(II)(ONO)* complex by photoreduction of the ferric precursor crystals using high-intensity X-ray radiation. PubMed: 20568729DOI: 10.1021/bi100801g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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