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- W2186013708 abstract "Recombinant protein was prepared as described [2, 3]. The crystal of Fe(II)-O2 complex was formed using sitting drop vapor diffusion method, 1.9-2.1 M ammonium citrate, pH 7.0 as a precipitant for 3-4 days at 20 °C. Crystals grew in space group P6522 with unit cell dimensions a = b = 69.4 A, c = 353.8 A, with two molecules per asymmetric unit and a solvent content of 71%. The structure of Tp trHb was solved using the molecular replacement method. Results O2 association and dissociation rate constants of Tp trHb were determined to 5.5 μM –1 s –1 , and 0.18 s –1 , respectively. The Kd value of Tp trHb was 33 nM. The autoxidation rate was determined to 3.8 × 10 –3 h –1 . These values are comparable to those of HbN from Mycobacterium tuberculosis. To understand the molecular mechanism of O2 stability, we solved the crystal structure of Fe(II)-O2 complex of Tp trHb. There were two molecules of Tp trHb in an asymmetric unit. Tp trHb showed typical 2/2 α-helical sandwich fold. Nterminal 4 residues were not modeled because of poor electron density. Heme was coordinated to His73, and further stabilized with hydrogen bond between Thr41 OG1 and heme propionate O2A, and main chain nitrogen of Lys67 and heme propionate O1D (Figure 1). Figrue 1: Active site structures of Fe(II)-O2 complex of Tp trHb. The Fo–Fc omit map contoured at 3.0σ for oxygen molecule is also shown. Hydrogen bonds are shown by dashed lines. The atomic color scheme for amino acids is: carbon, green; nitrogen, blue; and oxygen, red." @default.
- W2186013708 created "2016-06-24" @default.
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- W2186013708 date "2011-01-01" @default.
- W2186013708 modified "2023-09-27" @default.
- W2186013708 title "Crystal structure of Group I truncated hemoglobin from Tetrahymena pyriformis" @default.
- W2186013708 hasPublicationYear "2011" @default.
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