7L3Y
Crystal structure of oxy-I107E CuB myoglobin (I107E L29H F43H sperm whale myoglobin; partial occupancy)
Summary for 7L3Y
| Entry DOI | 10.2210/pdb7l3y/pdb |
| Related | 7KYR |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, PEROXIDE ION, ... (5 entities in total) |
| Functional Keywords | globin, oxidase, oxygen binding, oxygen reduction, oxidoreductase, oxygen transport |
| Biological source | Physeter catodon (Sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18082.01 |
| Authors | Petrik, I.,Lu, Y. (deposition date: 2020-12-18, release date: 2021-02-03, Last modification date: 2023-10-18) |
| Primary citation | Petrik, I.D.,Davydov, R.,Kahle, M.,Sandoval, B.,Dwaraknath, S.,Adelroth, P.,Hoffman, B.,Lu, Y. An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network. Biochemistry, 60:346-355, 2021 Cited by PubMed Abstract: Efficiently carrying out the oxygen reduction reaction (ORR) is critical for many applications in biology and chemistry, such as bioenergetics and fuel cells, respectively. In biology, this reaction is carried out by large, transmembrane oxidases such as heme-copper oxidases (HCOs) and cytochrome oxidases. Common to these oxidases is the presence of a glutamate residue next to the active site, but its precise role in regulating the oxidase activity remains unclear. To gain insight into its role, we herein report that incorporation of glutamate next to a designed heme-copper center in two biosynthetic models of HCOs improves O binding affinity, facilitates protonation of reaction intermediates, and eliminates release of reactive oxygen species. High-resolution crystal structures of the models revealed extended, water-mediated hydrogen-bonding networks involving the glutamate. Electron paramagnetic resonance of the cryoreduced oxy-ferrous centers at cryogenic temperature followed by thermal annealing allowed observation of the key hydroperoxo intermediate that can be attributed to the hydrogen-bonding network. By demonstrating these important roles of glutamate in oxygen reduction biochemistry, this work offers deeper insights into its role in native oxidases, which may guide the design of more efficient artificial ORR enzymes or catalysts for applications such as fuel cells. PubMed: 33464878DOI: 10.1021/acs.biochem.0c00852 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.18 Å) |
Structure validation
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