Document Detail


Monooxygenase activity of Octopus vulgaris hemocyanin.
MedLine Citation:
PMID:  18553939     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Octopus vulgaris hemocyanin ( Ov-Hc) and one of its minimal functional units ( Ov-g) have been purified, and their spectroscopic features and monooxygenase (phenolase) activity have been examined in detail. The oxy forms of both Ov-Hc and Ov-g are stable in 0.5 M borate buffer (pH 9.0) even in the presence of a high concentration of urea at 25 degrees C; approximately 90 and approximately 75% of the (mu-eta (2):eta (2)-peroxo)dicopper(II) species of Ov-Hc and Ov-g, respectively, remained unchanged after argon (Ar) gas flushing of the sample solutions for 1 h. The catalytic activity of Ov-g in the oxygenation reaction (multiturnover reaction) of 4-methylphenol ( p-cresol) to 4-methyl-1,2-dihydroxybenzene (4-methylcatechol) was higher than that of Ov-Hc, and its catalytic activity was further accelerated by the addition of urea. Kinetic deuterium isotope effect analysis and Hammett analysis using a series of phenol derivatives under anaerobic conditions (single-turnover reaction) have indicated that the monooxygenation reaction of phenols to catechols by the peroxo species of oxyhemocyanin proceeds via electrophilic aromatic substitution mechanism as in the case of tyrosinase. The effect of urea on the redox functions of oxyhemocyanin is discussed on the basis of the spectroscopic analysis and reactivity studies.
Authors:
Kenji Suzuki; Chizu Shimokawa; Chiyuki Morioka; Shinobu Itoh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-06-14
Journal Detail:
Title:  Biochemistry     Volume:  47     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-07-01     Completed Date:  2008-07-16     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7108-15     Citation Subset:  IM    
Affiliation:
Department of Chemistry, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan.
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MeSH Terms
Descriptor/Qualifier:
Aerobiosis
Anaerobiosis
Animals
Binding Sites
Catalysis
Catechols / chemistry,  metabolism
Circular Dichroism
Hemocyanin / chemistry,  metabolism*
Mixed Function Oxygenases / chemistry,  metabolism*
Octopodiformes / enzymology*
Phenols / chemistry,  metabolism
Protein Structure, Quaternary
Substrate Specificity
Time Factors
Chemical
Reg. No./Substance:
0/Catechols; 0/Phenols; 0/oxy-beta-hemocyanin; 9013-72-3/Hemocyanin; EC 1.-/Mixed Function Oxygenases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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