氣態蛋白質構形和蛋白質與輔基間的鍵能探討

A Combined Study with FTICR Mass Spectrometry and IR Laser Spectroscopy: Dissociation of Heme from Gaseous Myoglobin Ions

高靜民(Ching-Min Kao)

指導教授 ： 李遠哲

共同指導教授 ： 張煥正(Huan-Cheng Chang)

國立臺灣大學/理學院/化學研究所/碩士(2005年)

https://doi.org/10.6342/NTU.2005.01418

摘要

無資料

關鍵字

蛋白質構形 ； 鍵能 ； 傅立葉轉換質譜儀 ； 原血紅素 ； 肌紅蛋白 ； 血紅素 ； 紅外多光子解離

並列摘要

Detachment of heme prosthetic groups from gaseous myoglobin and
hemoglobin ions by Collision-Induced Dissociation (CID) and InfraRed
MultiPhoton Dissociation (IRMPD) has been investigated by Fourier-Transform
Ion Cyclotron Resonance (FT-ICR) mass spectrometry. Multiply charged
holomyoglobin (hMb) or holohemoglobin (hHb) ions were generated by
electrospray ionization and transferred into the ICR cell, where the ions of interest
(hMb10+, for example) were isolated, excited translationally and collided with
pulsed Ar gas or heated with IR laser, producing apomyoglobin (aMb) or
apohemoglobin (aHb) ions. Dissociation energies of ~0.9 eV and ~0.7 eV were
determined for myogloin and hemoglobin. Multiply charged hemoglobins were
applied to IRMPD, such that the OPO laser was fired into the ICR cell and heated
up the myoglobin to the point of dissociation. The dissociation energy of
myoglobin from IRMPD is thus measured. Two techniques, IRMPD and CID,
which have a similar nature of ion activation, are applied on hemoproteins and
compared on a collateral level. The measured results concur with the previous
Blackbody Infrared Radiative Dissociation method.
Tunable OPO laser is directed on the myoglobin ions in the ICR cell and
generates the first myoglobin spectroscopy in the gas phase. From the
spectroscopy, the charge dependant hemoprotein unfolding process was suggested,
displaying the C-H and free N-H bonds. The infrared spectroscopic evidence of
gaseous myoglobin is thus presented for the first time.

並列關鍵字

Fourier transform ion cyclotron resonance mass spectrometer ； dissocation energy ； myoglobin ； hemoglobin ； heme ； InfraRed MultiPhoton Dissociation ； CID

參考文獻

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