5SYD
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5HAV
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7KYR
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7L3Y
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7L3U
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4TYX
| Structure of aquoferric sperm whale myoglobin L29H/F33Y/F43H/S92A mutant | Descriptor: | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Bhagi-Damodaran, A, Petrik, I.D, Robinson, H, Lu, Y. | Deposit date: | 2014-07-09 | Release date: | 2014-08-13 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (1.64 Å) | Cite: | Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin. J.Am.Chem.Soc., 136, 2014
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4MXL
| X-ray structure of ZnPFeBMb1 | Descriptor: | Myoglobin, PROTOPORPHYRIN IX CONTAINING ZN | Authors: | Chakraborty, S, Lu, Y, Petrik, I. | Deposit date: | 2013-09-26 | Release date: | 2014-02-12 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Spectroscopic and computational study of a nonheme iron nitrosyl center in a biosynthetic model of nitric oxide reductase. Angew.Chem.Int.Ed.Engl., 53, 2014
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4MXK
| X-ray structure of Fe(II)-ZnPIXFeBMb1 | Descriptor: | FE (II) ION, Myoglobin, PROTOPORPHYRIN IX CONTAINING ZN | Authors: | Chakraborty, S, Lu, Y, Petrik, I. | Deposit date: | 2013-09-26 | Release date: | 2014-02-12 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.52 Å) | Cite: | Spectroscopic and computational study of a nonheme iron nitrosyl center in a biosynthetic model of nitric oxide reductase. Angew.Chem.Int.Ed.Engl., 53, 2014
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5VNU
| Nonheme Iron Replacement in a Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Mn-bound FeBMb | Descriptor: | MANGANESE (II) ION, Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Reed, J, Shi, Y, Zhu, Q, Chakraborty, S, Mirs, E.N, Petrik, I.D, Bhagi-Damodaran, A, Ross, M, Moenne-Loccoz, P, Zhang, Y, Lu, Y. | Deposit date: | 2017-05-01 | Release date: | 2017-08-16 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (1.584 Å) | Cite: | Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism. J. Am. Chem. Soc., 139, 2017
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5VRT
| Nonheme Iron Replacement in a Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-bound FeBMb | Descriptor: | COBALT (II) ION, Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Reed, J, Shi, Y, Zhu, Q, Chakraborty, S, Mirs, E.N, Petrik, I.D, Bhagi-Damodaran, A, Ross, M, Moenne-Loccoz, P, Zhang, Y, Lu, Y. | Deposit date: | 2017-05-11 | Release date: | 2017-08-16 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.995 Å) | Cite: | Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism. J. Am. Chem. Soc., 139, 2017
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4FWZ
| Aquoferric CuB myoglobin (L29H F43H sperm whale myoglobin) | Descriptor: | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Gao, Y.-G, Robinson, H, Petrik, I.D, Miner, K.D, Lu, Y. | Deposit date: | 2012-07-02 | Release date: | 2012-07-18 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers. Angew.Chem.Int.Ed.Engl., 51, 2012
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4FWX
| Aquoferric F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) | Descriptor: | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Gao, Y.-G, Stoner-Ma, D, Robinson, H, Petrik, I.D, Miner, K.D, Lu, Y. | Deposit date: | 2012-07-02 | Release date: | 2012-07-18 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers. Angew.Chem.Int.Ed.Engl., 51, 2012
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4FWY
| F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound | Descriptor: | COPPER (II) ION, Myoglobin, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Gao, Y.-G, Robinson, H, Petrik, I.D, Miner, K.D, Lu, Y. | Deposit date: | 2012-07-02 | Release date: | 2012-07-18 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers. Angew.Chem.Int.Ed.Engl., 51, 2012
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