Noncovalent self-assembly of a heterotetrameric diiron protein

被引：55

作者：

Marsh, ENG

DeGrado, WF ^{[1
]}

机构：

[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

[2] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2002年 / 99卷 / 08期

关键词：

D O I：

10.1073/pnas.052023199

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Diiron and dimanganese proteins catalyze a wide range of hydrolytic and oxygen-dependent reactions, To probe the mechanisms by which individual members of this class of proteins are able to catalyze such a wide range of reactions, we have prepared a model four-helix bundle with a diiron site located near the center of the bundle. The four-helix bundle is constructed by the noncovalent self-assembly of three different chains (A(a), A(b), and B) that self-assemble into the desired heterotetramer when mixed in a 1:11:2 molar ratio. On addition of ferrous ions and oxygen, the protein forms a complex with a UV-visible spectrum closely resembling that of peroxo-bridged diferric species in natural proteins and model compounds. By combining a small collection of n variants of these peptides, it should now be possible to prepare an n(3) member library, which will allow systematic exploration of the features giving rise to the catalytic properties of this class of proteins.

引用

页码：5150 / 5154

页数：5

共 32 条

[1] The crystal structure of an azide complex of the diferrous R2 subunit of ribonucleotide reductase displays a novel carboxylate shift with important mechanistic implications for diiron-catalyzed oxygen activation [J].