, volume 29 , issue 5 , pages 492-494

The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase

Maria G. Khrenova ^{1, 2}

V. S. Tsirel’son ^{2, 3}

Hide authors affiliations Show authors affiliations: 3 affiliations

Department of Chemistry, M. V. Lomonosov Moscow State University, 119991 Moscow, Russian Federation |

Federal Research Centre ‘Fundamentals of Biotechnology’, Russian Academy of Sciences, 119071 Moscow, Russian Federation |

D. I. Mendeleev University of Chemical Technology of Russia, 125047 Moscow, Russian Federation |

Publication type: Journal Article

Publication date: 2019-09-01

OOO Zhurnal "Mendeleevskie Soobshcheniya"

Mendeleev Communications

scimago Q3

wos Q3

SJR: 0.305

CiteScore: 3.0

Impact factor: 1.7

ISSN: 09599436, 1364551X

DOI: 10.1016/j.mencom.2019.09.004

Copy DOI

General Chemistry

Abstract

The combined quantum mechanics/molecular mechanics investigation followed by the detailed electron density analysis for 9 cephalosporin–L1 metallo-β-lactamase complexes revealed correlation between the N···H hydrogen bond strength in the transition state at the limiting step and the reactivity of cephalosporin compounds. The stronger interactions were typical of the less reactive species.

Found

4 citations

Levina Elena

20 publications, 264 citations, 3 reviews

h-index: 9

Kurnakov Institute of General and Inorganic Chemistry of the Russian Academy of Sciences

Moscow Institute of Physics and Technology

Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Research interests

Computational chemistry

Molecular dynamics

Physical Chemistry

Quantum Chemistry

1 citation

Kulakova Anna

PhD in Physics and Mathematics

37 publications, 131 citations

h-index: 6

Lomonosov Moscow State University

Research interests

Molecular modeling

Reaction mechanisms

Top-30

Journals

	1 2 3 4 5
Mendeleev Communications	Mendeleev Communications, 5, 31.25% Mendeleev Communications 5 publications, 31.25%
Russian Chemical Reviews	Russian Chemical Reviews, 2, 12.5% Russian Chemical Reviews 2 publications, 12.5%
International Journal of Quantum Chemistry	International Journal of Quantum Chemistry, 1, 6.25% International Journal of Quantum Chemistry 1 publication, 6.25%
Biochemistry (Moscow)	Biochemistry (Moscow), 1, 6.25% Biochemistry (Moscow) 1 publication, 6.25%
Russian Journal of Physical Chemistry A	Russian Journal of Physical Chemistry A, 1, 6.25% Russian Journal of Physical Chemistry A 1 publication, 6.25%
RSC Advances	RSC Advances, 1, 6.25% RSC Advances 1 publication, 6.25%
Molecules	Molecules, 1, 6.25% Molecules 1 publication, 6.25%
Russian Journal of Physical Chemistry B	Russian Journal of Physical Chemistry B, 1, 6.25% Russian Journal of Physical Chemistry B 1 publication, 6.25%
Journal of Physical Chemistry A	Journal of Physical Chemistry A, 1, 6.25% Journal of Physical Chemistry A 1 publication, 6.25%
Journal of Chemical Information and Modeling	Journal of Chemical Information and Modeling, 1, 6.25% Journal of Chemical Information and Modeling 1 publication, 6.25%
Coordination Chemistry Reviews	Coordination Chemistry Reviews, 1, 6.25% Coordination Chemistry Reviews 1 publication, 6.25%
	1 2 3 4 5

Publishers

	1 2 3 4 5
OOO Zhurnal "Mendeleevskie Soobshcheniya"	OOO Zhurnal "Mendeleevskie Soobshcheniya", 5, 31.25% OOO Zhurnal "Mendeleevskie Soobshcheniya" 5 publications, 31.25%
Pleiades Publishing	Pleiades Publishing, 3, 18.75% Pleiades Publishing 3 publications, 18.75%
Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii	Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii, 2, 12.5% Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii 2 publications, 12.5%
American Chemical Society (ACS)	American Chemical Society (ACS), 2, 12.5% American Chemical Society (ACS) 2 publications, 12.5%
Wiley	Wiley, 1, 6.25% Wiley 1 publication, 6.25%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 1, 6.25% Royal Society of Chemistry (RSC) 1 publication, 6.25%
MDPI	MDPI, 1, 6.25% MDPI 1 publication, 6.25%
Elsevier	Elsevier, 1, 6.25% Elsevier 1 publication, 6.25%
	1 2 3 4 5

We do not take into account publications without a DOI.
Statistics recalculated weekly.

Are you a researcher?

Create a profile to get free access to personal recommendations for colleagues and new articles.

Metrics

Cite this

GOST |

Cite this

GOST Copy

Khrenova M. G. et al. The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase // Mendeleev Communications. 2019. Vol. 29. No. 5. pp. 492-494.

GOST all authors (up to 50) Copy

Khrenova M. G., Tsirel’son V. S. The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase // Mendeleev Communications. 2019. Vol. 29. No. 5. pp. 492-494.

RIS |

Cite this

RIS Copy

TY - JOUR

DO - 10.1016/j.mencom.2019.09.004

UR - https://doi.org/10.1016/j.mencom.2019.09.004

TI - The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase

T2 - Mendeleev Communications

AU - Khrenova, Maria G.

AU - Tsirel’son, V. S.

PY - 2019

DA - 2019/09/01

PB - OOO Zhurnal "Mendeleevskie Soobshcheniya"

SP - 492-494

IS - 5

VL - 29

SN - 0959-9436

SN - 1364-551X

ER -

BibTex |

Cite this

BibTex (up to 50 authors) Copy

@article{2019_Khrenova,

author = {Maria G. Khrenova and V. S. Tsirel’son},

title = {The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase},

journal = {Mendeleev Communications},

year = {2019},

volume = {29},

publisher = {OOO Zhurnal "Mendeleevskie Soobshcheniya"},

month = {sep},

url = {https://doi.org/10.1016/j.mencom.2019.09.004},

number = {5},

pages = {492--494},

doi = {10.1016/j.mencom.2019.09.004}

}

MLA

Cite this

MLA Copy

Khrenova, Maria G., et al. “The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase.” Mendeleev Communications, vol. 29, no. 5, Sep. 2019, pp. 492-494. https://doi.org/10.1016/j.mencom.2019.09.004.

Publisher

OOO Zhurnal "Mendeleevskie Soobshcheniya"

Journal

Mendeleev Communications

scimago Q3

wos Q3

SJR

0.305

CiteScore

3.0

Impact factor

1.7

ISSN

09599436 (Print)

1364551X (Electronic)

Labs

Laboratory of Quantum Chemistry and Molecular Modeling

Profiles