A new measurement system for UV resonance Raman spectra of large proteins and its application to cytochrome c oxidase

被引:36
作者
Aki, M
Ogura, T
Shinzawa-Itoh, K
Yoshikawa, S
Kitagawa, T [1 ]
机构
[1] Grad Univ Adv Studies, Sch Math & Phys Sci, Okazaki, Aichi 4448585, Japan
[2] Univ Tokyo, Grad Sch Arts & Sci, Meguro Ku, Tokyo 1538902, Japan
[3] Japan Sci & Technol, CREST, Kamigori, Hyogo 6781297, Japan
[4] Himeji Inst Technol, Dept Life Sci, Kamigori, Hyogo 6781297, Japan
[5] Okazaki Natl Res Inst, Inst Mol Sci, Okazaki, Aichi 4448585, Japan
关键词
D O I
10.1021/jp000357p
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
A new type of ultraviolet resonance Raman (UVRR) measurement system suitable to a limited amount of large protein samples is proposed and the results from its application to bovine cytochrome c oxidase (CcO) is presented. To minimize the sample damage caused by high-flux UV laser illumination and to reject visible fluorescence from the sample, frequency-doubling of a mode-locked Ar+ ion laser and a solar blind multichannel detector were employed, respectively. A new spinning cell was designed so that the sample solution could be stirred during spinning of the cell. Combination of all these devices resulted in successful observation of high quality UVRR spectra of CcO excited at 244 nm. The RR bands of tryptophan and tyrosine residues dominated the observed spectra, while an extra band appeared at 1656 cm(-1). The frequency of the extra band as well as those of all other bands were unaltered by the redox change of metal centers and ligand binding to heme a(3). Deprotonation of a tyrosine residue(s) with a low pK(a) value was detected for the resting state at pH 9.1. Examination of all possible assignments led us to conclude that the extra band arose from the linoleoyl side chain of phospholipids and its intensity suggested the presence of 21 linoleoyl groups per CcO molecule.
引用
收藏
页码:10765 / 10774
页数:10
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