High Thermal Stability and Unique Trimer Formation of Cytochrome c′ from Thermophilic Hydrogenophilus thermoluteolus

被引：12
|
作者：
Fujii, Sotaro [1 ]
Masanari, Misa [1 ]
Inoue, Hiroki [1 ]
Yamanaka, Masaru [2 ]
Wakai, Satoshi [1 ]
Nishihara, Hirofumi [3 ]
Sambongi, Yoshihiro [1 ]
机构：
[1] Hiroshima Univ, Grad Sch Biosphere Sci, Hiroshima 7398528, Japan
[2] Nara Inst Sci & Technol, Grad Sch Mat Sci, Nara 6300192, Japan
[3] Ibaraki Univ, Fac Agr, Ami, Ibaraki 3000393, Japan
来源：
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2013年 / 77卷 / 08期
关键词：
cytochrome c '; mesophile; protein stability; thermophile; trimer; ESCHERICHIA-COLI; OXIDIZING BACTERIUM; HEME; PROTEIN; THERMOSTABILITY; BIOGENESIS; CUTA1;
D O I：
10.1271/bbb.130226
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Sequence analysis indicated that thermophilic Hydrogenophilus thermoluteolus cytochrome c' (PHCP) and its mesophilic homolog, Allochromatium vinosum cytochrome c' (AVCP), closely resemble each other in a phylogenetic tree of the cytochrome c' family, with 55% sequence identity. The denaturation temperature of PHCP was 87 degrees C, 35 degrees C higher than that of AVCP. Furthermore, PHCP exhibited a larger enthalpy change value during its thermal denaturation than AVCP. While AVCP was dimeric, as observed previously, PHCP was trimeric, and this was the first observation as a cytochrome c'. Dissociation of trimeric PHCP and its protein denaturation reversibly occurred at the same time in a two-state transition manner. Therefore, PHCP is enthalpically more stable than AVCP, perhaps due to its unique trimeric form, in addition to the lower number of Gly residues in its putative at-helical regions.
引用
收藏
页码：1677 / 1681
页数：5
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