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Mono-oxygenase Enzymes and Their Simulation

Afanasii Andreevich Akhrem 1
Afanasii Andreevich Akhrem
, 
Dmitrii Ivanovich Metelitsa 1
Dmitrii Ivanovich Metelitsa
, 
M E Skurko 1
M E Skurko
1 Institute of Bioorganic Chemistry of the Academy of Sciences Byelorussian SSR, Minsk
Published 30 November 1974
Communication , Volume 44, Issue 5, 398-412
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Akhrem A. A., Metelitsa D. I., Skurko M. E. Mono-oxygenase Enzymes and Their Simulation // Russian Chemical Reviews. 1975. Vol. 44. No. 5. pp. 398-412.
GOST all authors (up to 50)
Akhrem A. A., Metelitsa D. I., Skurko M. E. Mono-oxygenase Enzymes and Their Simulation // Russian Chemical Reviews. 1975. Vol. 44. No. 5. pp. 398-412.
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TY - JOUR
DO - 10.1070/RC1975v044n05ABEH002350
UR - https://rcr.colab.ws/publications/10.1070/RC1975v044n05ABEH002350
TI - Mono-oxygenase Enzymes and Their Simulation
T2 - Russian Chemical Reviews
AU - Akhrem, Afanasii Andreevich
AU - Metelitsa, Dmitrii Ivanovich
AU - Skurko, M E
PY - 1975
DA - 1974/11/30
PB - ANO Editorial Board of the journal Uspekhi Khimii
SP - 398-412
IS - 5
VL - 44
ER -
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BibTex (up to 50 authors)
@article{1975_Akhrem,
author = {Afanasii Andreevich Akhrem and Dmitrii Ivanovich Metelitsa and M E Skurko},
title = {Mono-oxygenase Enzymes and Their Simulation},
journal = {Russian Chemical Reviews},
year = {1975},
volume = {44},
publisher = {ANO Editorial Board of the journal Uspekhi Khimii},
month = {Nov},
url = {https://rcr.colab.ws/publications/10.1070/RC1975v044n05ABEH002350},
number = {5},
pages = {398--412},
doi = {10.1070/RC1975v044n05ABEH002350}
}
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MLA
Akhrem, Afanasii Andreevich, et al. “Mono-oxygenase Enzymes and Their Simulation.” Russian Chemical Reviews, vol. 44, no. 5, Nov. 1975, pp. 398-412. https://rcr.colab.ws/publications/10.1070/RC1975v044n05ABEH002350.
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Abstract

Information on reactions catalysed by mono-oxygenases is summarised and classified. The composition and properties of these enzymes are considered, together with the kinetics and the mechanism of their action in the hydroxylation of aliphatic and aromatic compounds and in the epoxidation of alkenes. Methods for imitating the action of mono-oxygenases are discussed and systematised, and the reaction mechanisms of the model systems are examined critically.
A list of 193 references is included.