Catalytic Cycle of Multicopper Oxidases Studied by Combined Quantum- and Molecular-Mechanical Free-Energy Perturbation Methods.
(2015) In The Journal of Physical Chemistry Part B 119(26). p.8268-8284- Abstract
- We have used combined quantum mechanical and molecular mechanical free-energy perturbation methods in combination with explicit solvent simulations to study the reaction mechanism of the multicopper oxidases, in particular, the regeneration of the reduced state from the native intermediate. For 52 putative states of the trinuclear copper cluster, differing in the oxidation states of the copper ions and the protonation states of water- and O2-derived ligands, we have studied redox potentials, acidity constants, isomerization reactions, as well as water- and O2 binding reactions. Thereby, we can propose a full reaction mechanism of the multicopper oxidases with atomic detail. We also show that the two copper sites in the protein communicate... (More)
- We have used combined quantum mechanical and molecular mechanical free-energy perturbation methods in combination with explicit solvent simulations to study the reaction mechanism of the multicopper oxidases, in particular, the regeneration of the reduced state from the native intermediate. For 52 putative states of the trinuclear copper cluster, differing in the oxidation states of the copper ions and the protonation states of water- and O2-derived ligands, we have studied redox potentials, acidity constants, isomerization reactions, as well as water- and O2 binding reactions. Thereby, we can propose a full reaction mechanism of the multicopper oxidases with atomic detail. We also show that the two copper sites in the protein communicate so that redox potentials and acidity constants of one site are affected by up to 0.2 V or 3 pKa units by a change in the oxidation state of the other site. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7508396
- author
- Li, Jilai LU ; Farrokhnia, Maryam LU ; Rulisek, Lubomir and Ryde, Ulf LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Part B
- volume
- 119
- issue
- 26
- pages
- 8268 - 8284
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:26039490
- wos:000357623400005
- scopus:84947465829
- pmid:26039490
- ISSN
- 1520-5207
- DOI
- 10.1021/acs.jpcb.5b02864
- 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
- 752a1693-99d8-4dce-b26b-4459dfe37856 (old id 7508396)
- date added to LUP
- 2016-04-01 10:57:28
- date last changed
- 2023-03-17 18:34:48
@article{752a1693-99d8-4dce-b26b-4459dfe37856, abstract = {{We have used combined quantum mechanical and molecular mechanical free-energy perturbation methods in combination with explicit solvent simulations to study the reaction mechanism of the multicopper oxidases, in particular, the regeneration of the reduced state from the native intermediate. For 52 putative states of the trinuclear copper cluster, differing in the oxidation states of the copper ions and the protonation states of water- and O2-derived ligands, we have studied redox potentials, acidity constants, isomerization reactions, as well as water- and O2 binding reactions. Thereby, we can propose a full reaction mechanism of the multicopper oxidases with atomic detail. We also show that the two copper sites in the protein communicate so that redox potentials and acidity constants of one site are affected by up to 0.2 V or 3 pKa units by a change in the oxidation state of the other site.}}, author = {{Li, Jilai and Farrokhnia, Maryam and Rulisek, Lubomir and Ryde, Ulf}}, issn = {{1520-5207}}, language = {{eng}}, number = {{26}}, pages = {{8268--8284}}, publisher = {{The American Chemical Society (ACS)}}, series = {{The Journal of Physical Chemistry Part B}}, title = {{Catalytic Cycle of Multicopper Oxidases Studied by Combined Quantum- and Molecular-Mechanical Free-Energy Perturbation Methods.}}, url = {{https://lup.lub.lu.se/search/files/2265272/8508851.pdf}}, doi = {{10.1021/acs.jpcb.5b02864}}, volume = {{119}}, year = {{2015}}, }