Non-covalent interactions in the glutathione peroxidase active center and their influence on the enzyme activity

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Non-covalent interactions in the glutathione peroxidase active center and their influence on the enzyme activity. / Tupikina, Elena Yu.

In: Organic and Biomolecular Chemistry, Vol. 20, No. 28, 29.06.2022, p. 5551-5557.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{4a055cbb2046487183d7420b7d6ea856,

title = "Non-covalent interactions in the glutathione peroxidase active center and their influence on the enzyme activity",

abstract = "In this computational work, the structure of the active center of the enzyme glutathione peroxidase (in three forms -SeH, -SeOH and -Se(O)OH) and the non-covalent interactions in it were investigated using modern quantum chemistry methods. The non-covalent interactions are described in detail. The presence of σ-hole interactions (chalcogen, tetrel and pnictogen bonds) formed mostly by a selenium atom as an electrophile in the glutathione peroxidase active center is confirmed for the first time. It is shown that a number of non-covalent interactions stabilize intermediates along the catalytic cycle and that modelling of the whole enzyme active center is necessary for accurate predictions of thermodynamic parameters, in particular, activation barriers.",

keywords = "Catalysis, Glutathione Peroxidase, Selenium, Thermodynamics",

author = "Tupikina, {Elena Yu}",

note = "Publisher Copyright: {\textcopyright} 2022 The Royal Society of Chemistry.",

year = "2022",

month = jun,

day = "29",

doi = "10.1039/d2ob00890d",

language = "English",

volume = "20",

pages = "5551--5557",

journal = "Organic and Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

number = "28",

}

RIS

TY - JOUR

T1 - Non-covalent interactions in the glutathione peroxidase active center and their influence on the enzyme activity

AU - Tupikina, Elena Yu

PY - 2022/6/29

Y1 - 2022/6/29

N2 - In this computational work, the structure of the active center of the enzyme glutathione peroxidase (in three forms -SeH, -SeOH and -Se(O)OH) and the non-covalent interactions in it were investigated using modern quantum chemistry methods. The non-covalent interactions are described in detail. The presence of σ-hole interactions (chalcogen, tetrel and pnictogen bonds) formed mostly by a selenium atom as an electrophile in the glutathione peroxidase active center is confirmed for the first time. It is shown that a number of non-covalent interactions stabilize intermediates along the catalytic cycle and that modelling of the whole enzyme active center is necessary for accurate predictions of thermodynamic parameters, in particular, activation barriers.

AB - In this computational work, the structure of the active center of the enzyme glutathione peroxidase (in three forms -SeH, -SeOH and -Se(O)OH) and the non-covalent interactions in it were investigated using modern quantum chemistry methods. The non-covalent interactions are described in detail. The presence of σ-hole interactions (chalcogen, tetrel and pnictogen bonds) formed mostly by a selenium atom as an electrophile in the glutathione peroxidase active center is confirmed for the first time. It is shown that a number of non-covalent interactions stabilize intermediates along the catalytic cycle and that modelling of the whole enzyme active center is necessary for accurate predictions of thermodynamic parameters, in particular, activation barriers.

KW - Catalysis

KW - Glutathione Peroxidase

KW - Selenium

KW - Thermodynamics

UR - http://www.scopus.com/inward/record.url?scp=85133963740&partnerID=8YFLogxK

U2 - 10.1039/d2ob00890d

DO - 10.1039/d2ob00890d

M3 - Article

C2 - 35791825

AN - SCOPUS:85133963740

VL - 20

SP - 5551

EP - 5557

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 28

ER -

ID: 97765638