Two-dimensional crystallization of monomeric bovine cytochromecoxidase with bound cytochromecin reconstituted lipid membranes | Zendy

Yukiho Osuda | Zendy; Kyoko ShinzawaItoh | Zendy; Kazutoshi Tani | Zendy; Shintaro Maeda | Zendy; Shinya Yoshikawa | Zendy; Tomitake Tsukihara | Zendy; Christoph Gerle | Zendy

Open Access

Two-dimensional crystallization of monomeric bovine cytochromecoxidase with bound cytochromecin reconstituted lipid membranes

Author(s) -

Yukiho Osuda,

Kyoko ShinzawaItoh,

Kazutoshi Tani,

Shintaro Maeda,

Shinya Yoshikawa,

Tomitake Tsukihara,

Christoph Gerle

Publication year - 2016

Publication title -

microscopy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.545

H-Index - 52

eISSN - 2050-5701

pISSN - 2050-5698

DOI - 10.1093/jmicro/dfv381

Subject(s) - cytochrome c oxidase , cytochrome , electron transport complex iv , cytochrome c , chemistry , electron transport chain , membrane , monomer , crystallization , cytochrome c1 , inner mitochondrial membrane , biophysics , oxidase test , oxygen , crystallography , mitochondrion , coenzyme q – cytochrome c reductase , biochemistry , enzyme , biology , organic chemistry , polymer

Mitochondrial cytochrome c oxidase utilizes electrons provided by cytochrome c for the active vectorial transport of protons across the inner mitochondrial membrane through the reduction of molecular oxygen to water. Direct structural evidence on the transient cytochrome c oxidase-cytochrome c complex thus far, however, remains elusive and its physiological relevant oligomeric form is unclear. Here, we report on the 2D crystallization of monomeric bovine cytochrome c oxidase with tightly bound cytochrome c at a molar ratio of 1:1 in reconstituted lipid membranes at the basic pH of 8.5 and low ionic strength.

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