Characterization of a partially unfolded high potential iron protein

被引：66

作者：

Bertini, I

Cowan, JA

Luchinat, C

Natarajan, K

Piccioli, M

机构：

[1] OHIO STATE UNIV, DEPT CHEM, EVANS LAB CHEM, COLUMBUS, OH 43210 USA

[2] UNIV FLORENCE, DEPT SOIL CHEM & PLANT NUTR, I-50144 FLORENCE, ITALY

来源：

BIOCHEMISTRY | 1997年 / 36卷 / 31期

关键词：

D O I：

10.1021/bi970810w

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：

A partially unfolded state of the Fe4S4-containing high potential iron-sulfur protein from Chromatium vinosum has been detected and characterized by NMR spectroscopy following addition of a concentrated solution of guanidinium chloride to the native protein. This intermediate species (i) maintains the polymetallic center, (ii) exhibits a largely collapsed secondary structure, and (iii) undergoes East cluster decomposition upon oxidation. This information is framed into the knowledge about this class of proteins, and the possible role of this intermediate with respect to the in vivo folding/unfolding process is discussed as well its role in the slow hydrolytic degradation characteristic of oxidized HiPIPs.

引用

页码：9332 / 9339

页数：8

共 68 条

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