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- W2419565362 abstract "In this report, the structure and the binding characteristics of ferri-heme as well as its complex with myoglobin have been studied by using collision-induced dissociation (CID) method in a Fourier-transform ion cyclotron resonance (FT-ICR) cell. Performing on-resonance RF excitation to the selective precursor, we monitored the dependencies of product yields of CID as a function of ion energies and determined their dissociation thresholds. By using this method, we determined unambiguously that the heme, as a major oxygen-binding site of haemprotein, is only loosely bound to myoglobin with dissociation threshold of 1.0 ± 0.12 eV. Furthermore, an early dissociation started at 0.1 ± 0.03 eV suggesting the hMb ion contains two different conformers in our measurement. In applying it to the investigation of decomposition of Fe(III)-heme+, we determined that the decomposition of two carboxymethyl groups consecutively from it require threshold energies of respectively 2.3 ± 0.24 eV and 2.9 ± 0.27 eV. Moreover, the relative bond energy of its side chains is also obtained as: carboxymethyl groups < methyl groups < ethyl groups. Theoretical prediction carried out using density functional theory (DFT) method in both B3LYP/6-31G and B3LYP/6-311++G** level basis sets agree reasonably well with our observation. This method is unique in providing a rapid, non-selective, simple, and reliable qualitative measurement of dissociation energetics of both covalent and non-covalent interactions." @default.
- W2419565362 created "2016-06-24" @default.
- W2419565362 creator A5087037731 @default.
- W2419565362 date "2005-01-01" @default.
- W2419565362 modified "2023-09-24" @default.
- W2419565362 title "利用FT-ICR MS 探討蛋白質與輔基間的鍵結強度" @default.
- W2419565362 doi "https://doi.org/10.6342/ntu.2005.00439" @default.
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