Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6680
Title: Structure of the heme o prosthetic group from the terminal quinol oxidase of escherichia coli
Authors: Wu, Wei
Chang, Chi
Varotsis, Constantinos 
Keywords: Heme
Escherichia coli
Cytochrome oxidase
Porphyrins
Oxygen
Enzymes
Issue Date: 1992
Publisher: ACS Publications
Source: Journal of the american chemical society, 1992, Volume 114, Issue 4, Pages 1182-1187
Abstract: The structure of the heme o prosthetic group of Escherichia coli quinol oxidase (cytochrome o oxidase) has been unambiguously determined by preparation and characterization of its iron-free derivative porphyrin o dimethyl ester, or dimethyl 2,7,12,18-tetramethyl-3-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12- trienyl]-8-vinylporphine-13,17-dipropionate. The identity of this natural porphyrin dimethyl ester was established by 1H NMR, MS, IR, and RR spectroscopies as well as by comparisons with model compounds and the closely related porphyrin a dimethyl ester. The reliability of the structure determination was further strengthened by the isolation and characterization of the acetylated and dehydrated derivatives of porphyrin o
URI: http://ktisis.cut.ac.cy/handle/10488/6680
ISSN: 0002-7863 (print)
1520-5126 (online)
DOI: 10.1021/ja00030a009
Rights: © 1992 American Chemical Society
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