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Brief encounters of cytochrome c
Author(s) -
Lyons Joseph A,
Nissen Poul
Publication year - 2017
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201696124
Subject(s) - biology , cytochrome c oxidase , cytochrome c , electron transport complex iv , cytochrome , computational biology , protein structure , electron transfer , biochemistry , mitochondrion , enzyme , chemistry , organic chemistry
Transient protein interactions are paramount to life where fast and efficient transfer of information and cargo are often integral to pathways and networks. However, complexes formed by transient protein interactions are often times resistant to direct structural characterization due to their inherent, dynamic nature, so our knowledge to date typically derives from biochemical, biophysical and computational methods. In this issue, Shimada and co‐authors present the crystal structure of the mammalian cytochrome c oxidase in complex with its electron donor cytochrome c , identifying a new class of protein–protein interaction termed “soft and specific”.