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Title: How nature tunes isoenzyme activity in the multifunctional catalytic globin dehaloperoxidase from Amphitrite ornata

Authors:
; ; ;
Publication Date:
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1549085
Grant/Contract Number:  
W-31-109-Eng-38
Resource Type:
Publisher's Accepted Manuscript
Journal Name:
Biochimica et Biophysica Acta. Proteins and Proteomics
Additional Journal Information:
Journal Name: Biochimica et Biophysica Acta. Proteins and Proteomics Journal Volume: 1866 Journal Issue: 2; Journal ID: ISSN 1570-9639
Publisher:
Elsevier
Country of Publication:
France
Language:
English

Citation Formats

Carey, Leiah M., Gavenko, Roman, Svistunenko, Dimitri A., and Ghiladi, Reza A. How nature tunes isoenzyme activity in the multifunctional catalytic globin dehaloperoxidase from Amphitrite ornata. France: N. p., 2018. Web. doi:10.1016/j.bbapap.2017.11.004.
Carey, Leiah M., Gavenko, Roman, Svistunenko, Dimitri A., & Ghiladi, Reza A. How nature tunes isoenzyme activity in the multifunctional catalytic globin dehaloperoxidase from Amphitrite ornata. France. https://doi.org/10.1016/j.bbapap.2017.11.004
Carey, Leiah M., Gavenko, Roman, Svistunenko, Dimitri A., and Ghiladi, Reza A. Thu . "How nature tunes isoenzyme activity in the multifunctional catalytic globin dehaloperoxidase from Amphitrite ornata". France. https://doi.org/10.1016/j.bbapap.2017.11.004.
@article{osti_1549085,
title = {How nature tunes isoenzyme activity in the multifunctional catalytic globin dehaloperoxidase from Amphitrite ornata},
author = {Carey, Leiah M. and Gavenko, Roman and Svistunenko, Dimitri A. and Ghiladi, Reza A.},
abstractNote = {},
doi = {10.1016/j.bbapap.2017.11.004},
journal = {Biochimica et Biophysica Acta. Proteins and Proteomics},
number = 2,
volume = 1866,
place = {France},
year = {Thu Feb 01 00:00:00 EST 2018},
month = {Thu Feb 01 00:00:00 EST 2018}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1016/j.bbapap.2017.11.004

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Cited by: 10 works
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