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- W2082452016 abstract "HemAT is a signal transducer protein responsible for aerotaxis control of some bacteria and archaea, which contains a heme-containing globin domain as the sensor of its physiological effector, O 2 . The interaction between the heme-bound ligand and the surrounding amino acid residue(s) plays a crucial role for selective sensing of O 2 and signal transduction by HemAT. In this work, we have elucidated by resonance Raman spectroscopy how O 2 and CO interact with HemAT- Hs and HemAT- Rr , HemAT from Halobacterium salinarum and Rhodospirillum rubrum, respectively. HemAT- Hs and HemAT- Rr showed three conformers in the O 2 -bound form, as is the case of HemAT- Bs , HemAT from Bacillus subtilis. Though the hydrogen bonding patterns observed in the three conformers were the same for HemAT- Bs , HemAT- Hs , and HemAT- Rr , the involved residues for the hydrogen bonding interaction were different from one another." @default.
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- W2082452016 date "2008-02-01" @default.
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- W2082452016 title "Hydrogen bonding interaction on the heme-bound ligand in the heme-based O2 sensor protein" @default.
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- W2082452016 doi "https://doi.org/10.1142/s1088424608000182" @default.
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