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STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF CYTOCHROME-C-OXIDASE FROM PARACOCCUS-DENITRIFICANS
Author(s): IWATA S, OSTERMEIER C, LUDWIG B, MICHEL H
Source: NATURE    Volume: 376    Issue: 6542    Pages: 660-669    Published: AUG 24 1995  
Times Cited: 1,464     References: 46     
Abstract: The crystal structure at 2.8 Angstrom resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody F-v fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a(3)-copper B binuclear centre where molecular oxygen Is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.
Document Type: Article
Language: English
Addresses:
1. MAX PLANCK INST BIOPHYS, D-60528 FRANKFURT, GERMANY
2. UNIV FRANKFURT, BIOZENTRUM, INST BIOCHEM, D-60439 FRANKFURT, GERMANY
Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF
Subject Category: Multidisciplinary Sciences
IDS Number: RQ672
ISSN: 0028-0836
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