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High resolution X‐ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor
Author(s) -
Mirkin Nurit,
Jaconcic Jean,
Stojanoff Vivian,
Moreno Abel
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21452
Subject(s) - cytochrome c , electron transfer , crystallization , cytochrome , chemistry , biosensor , gene isoform , crystallography , resolution (logic) , protein crystallization , electron transport chain , globular protein , biophysics , biochemistry , biology , mitochondrion , enzyme , photochemistry , organic chemistry , computer science , artificial intelligence , gene
Abstract Cytochrome c is one of the most studied proteins probably due to its electron‐transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, M r 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 Å resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented. Proteins 2008. © 2007 Wiley‐Liss, Inc.