Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/2234
Title: Structure of the heme o prosthetic group from the terminal quinol oxidase of escherichia coli
Authors: Wu, Wei 
Chang, Chi 
Varotsis, Constantinos 
metadata.dc.contributor.other: Βαρώτσης, Κωνσταντίνος
Major Field of Science: Medical and Health Sciences
Keywords: Heme;Escherichia coli;Cytochrome oxidase;Porphyrins;Oxygen;Enzymes
Issue Date: 1992
Source: Journal of the american chemical society, 1992, vol. 114, no. 4, pp. 1182-1187
Volume: 114
Issue: 4
Start page: 1182
End page: 1187
Journal: Journal of the American Chemical Society 
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: https://hdl.handle.net/20.500.14279/2234
ISSN: 15205126
DOI: 10.1021/ja00030a009
Rights: © American Chemical Society
Type: Article
Affiliation: Michigan State University 
Affiliation : Michigan State University 
University of Helsinki 
Publication Type: Peer Reviewed
Appears in Collections:Άρθρα/Articles

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