ISSN:
1059-910X
Keywords:
Cytochrome oxidase
;
Electron microscopy
;
Image processing
;
Electron transport
;
Mitochondria
;
Membrane protein
;
Membrane structure
;
Protein structure
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Natural Sciences in General
Notes:
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 cryelectron microscopy and digital image processing. The structure of frozen-hydrated cytochrome oxidase dimers at 20 Å resolution is discussed as well as the packing of monomers within dimers and the site of cytochrome c binding. © 1994 Wiley-Liss, Inc.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jemt.1070270407
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