2FER
P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX
Summary for 2FER
| Entry DOI | 10.2210/pdb2fer/pdb |
| Related | 2FE6 2FEU |
| Descriptor | Cytochrome P450-cam, POTASSIUM ION, PROTOPORPHYRIN IX CONTAINING MN, ... (4 entities in total) |
| Functional Keywords | mono-oxygenase, heme, manganic, substrate-free, water cluster, oxidoreductase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 1 |
| Total formula weight | 47126.47 |
| Authors | von Koenig, K.,Makris, T.M.,Sligar, S.G.,Schlichting, I. (deposition date: 2005-12-16, release date: 2006-03-14, Last modification date: 2023-08-30) |
| Primary citation | Makris, T.M.,von Koenig, K.,Schlichting, I.,Sligar, S.G. The status of high-valent metal oxo complexes in the P450 cytochromes. J.Inorg.Biochem., 100:507-518, 2006 Cited by PubMed Abstract: The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented. PubMed: 16510191DOI: 10.1016/j.jinorgbio.2006.01.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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