High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor

被引：90

作者：

Mirkin, Nurit ^{[2
]}

Jaconcic, Jean ^{[3
]}

Stojanoff, Vivian ^{[3
]}

Moreno, Abel ^{[1
]}

机构：

[1] Univ Nacl Autonoma Mexico, Inst Quim, Mexico City 04510, DF, Mexico

[2] CUNY, Hunter Coll, New York, NY 10021 USA

[3] NSLS, Brookhaven Natl Lab, Upton, NY USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2008年 / 70卷 / 01期

关键词：

electrocrystallization; cytochrome c from bovine heart mitochondria; gel acupuncture method; atomic force microscopy; X-ray diffraction;

D O I：

10.1002/prot.21452

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：

Cytochrome c is one of the most studied protein., probably due to its electron-transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, M, 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well-studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 angstrom resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electro-crystallization and design of biosensors is presented.

引用

页码：83 / 92

页数：10

共 27 条

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