Cytochrome c oxidase: structural studies by electron microscopy of two-dimensional crystals.

Abstract:

:Cytochrome c oxidase is a complex integral membrane protein consisting of 13 different polypeptide chains and four metal centers having a total molecular weight of approximately 200,000 daltons. It can be isolated in two 2-dimensional crystalline forms differing in aggregation state of the enzyme. One crystal form consists of cytochrome oxidase dimers (approximately 400,000 daltons) embedded unidirectionally in the lipid bilayer of a collapsed vesicle while the other form consists of crystalline sheets of cytochrome oxidase monomers. Both crystal forms have been studied by electron microscopy during the past two decades, and this paper summarizes the results of early structural studies as well as more recent results applying techniques of cryoelectron microscopy and digital image processing. The structure of frozen-hydrated cytochrome oxidase dimers at 20 A resolution is discussed as well as the packing of monomers within dimers and the site of cytochrome c binding.

journal_name

Microsc Res Tech

authors

Frey TG

doi

10.1002/jemt.1070270407

subject

Has Abstract

pub_date

1994-03-01 00:00:00

pages

319-32

issue

4

eissn

1059-910X

issn

1097-0029

journal_volume

27

pub_type

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