Conversion of homocysteine to methionine by methionine synthase: a density functional study.
Jensen, Kasper LU and Ryde, Ulf LU
(2003)
In Journal of the American Chemical Society
125(46).
p.13970-13971
- Abstract
- This communication reports a theoretical study of the conversion of homocysteine to methionine by methionine synthase. The reaction pathway is based on density functional calculations with large basis sets, including thermodynamic, relativistic, and solvent effects. We find that the suggested SN2 mechanism explains well the experimentally observed reaction rate. The results show that the reaction is highly polar, as reflected in the change of charge density along the reaction coordinate. It is enhanced in the protein by two effects: deprotonation of the bound substrate and desolvation of substrate and cofactor in the rate-determining step.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/128721
- author
- Jensen, Kasper
LU
and Ryde, Ulf
LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of the American Chemical Society
- volume
- 125
- issue
- 46
- pages
- 13970 - 13971
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000186580600031
- scopus:0242666823
- pmid:14611228
- ISSN
- 1520-5126
- DOI
- 10.1021/ja034697a
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 3b019224-b231-47d6-8dff-0efff6bc7781 (old id 128721)
- date added to LUP
- 2016-04-01 16:12:55
- date last changed
- 2023-01-24 02:30:54
@article{3b019224-b231-47d6-8dff-0efff6bc7781,
abstract = {{This communication reports a theoretical study of the conversion of homocysteine to methionine by methionine synthase. The reaction pathway is based on density functional calculations with large basis sets, including thermodynamic, relativistic, and solvent effects. We find that the suggested SN2 mechanism explains well the experimentally observed reaction rate. The results show that the reaction is highly polar, as reflected in the change of charge density along the reaction coordinate. It is enhanced in the protein by two effects: deprotonation of the bound substrate and desolvation of substrate and cofactor in the rate-determining step.}},
author = {{Jensen, Kasper and Ryde, Ulf}},
issn = {{1520-5126}},
language = {{eng}},
number = {{46}},
pages = {{13970--13971}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of the American Chemical Society}},
title = {{Conversion of homocysteine to methionine by methionine synthase: a density functional study.}},
url = {{https://lup.lub.lu.se/search/files/135492234/61_ts.pdf}},
doi = {{10.1021/ja034697a}},
volume = {{125}},
year = {{2003}},
}