A QM/MM study of the nature of the entatic state in plastocyanin

Plastocyanin is a copper containing protein that is involved in the electron transfer process in photosynthetic organisms. The active site of plastocyanin is described as an entatic state whereby its structure represents a compromise between the structures favored by the oxidized and reduced forms....

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Main Authors: Hurd, Catherine A., Besley, Nicholas A., Robinson, David
Format: Article
Published: Wiley 2016
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Online Access:https://eprints.nottingham.ac.uk/38564/
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author Hurd, Catherine A.
Besley, Nicholas A.
Robinson, David
author_facet Hurd, Catherine A.
Besley, Nicholas A.
Robinson, David
author_sort Hurd, Catherine A.
building Nottingham Research Data Repository
collection Online Access
description Plastocyanin is a copper containing protein that is involved in the electron transfer process in photosynthetic organisms. The active site of plastocyanin is described as an entatic state whereby its structure represents a compromise between the structures favored by the oxidized and reduced forms. In this study the nature of the entatic state is investigated through density functional theory based hybrid quantum mechanics/molecular mechanics (QM/MM) molecular dynamics simulations. The strain energy is computed to be 12.8 kcal/mol and 14.5 kcal/mol for the oxidized and reduced forms of the protein, indicating that the active site has an intermediate structure. It is shown that the energy gap between the oxidized and reduced forms varies significantly with the fluctuations in the structure of the active site at room temperature. An accurate determination of the reorganization energy requires averaging over conformation and a large region of the protein around the active site to be treated at the quantum mechanical level.
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spelling nottingham-385642020-05-04T18:21:13Z https://eprints.nottingham.ac.uk/38564/ A QM/MM study of the nature of the entatic state in plastocyanin Hurd, Catherine A. Besley, Nicholas A. Robinson, David Plastocyanin is a copper containing protein that is involved in the electron transfer process in photosynthetic organisms. The active site of plastocyanin is described as an entatic state whereby its structure represents a compromise between the structures favored by the oxidized and reduced forms. In this study the nature of the entatic state is investigated through density functional theory based hybrid quantum mechanics/molecular mechanics (QM/MM) molecular dynamics simulations. The strain energy is computed to be 12.8 kcal/mol and 14.5 kcal/mol for the oxidized and reduced forms of the protein, indicating that the active site has an intermediate structure. It is shown that the energy gap between the oxidized and reduced forms varies significantly with the fluctuations in the structure of the active site at room temperature. An accurate determination of the reorganization energy requires averaging over conformation and a large region of the protein around the active site to be treated at the quantum mechanical level. Wiley 2016-11-14 Article PeerReviewed Hurd, Catherine A., Besley, Nicholas A. and Robinson, David (2016) A QM/MM study of the nature of the entatic state in plastocyanin. Journal of Computational Chemistry . ISSN 1096-987X QM/MM Electron transfer Plastocyanin http://onlinelibrary.wiley.com/doi/10.1002/jcc.24666/full doi:10.1002/jcc.24666 doi:10.1002/jcc.24666
spellingShingle QM/MM
Electron transfer
Plastocyanin
Hurd, Catherine A.
Besley, Nicholas A.
Robinson, David
A QM/MM study of the nature of the entatic state in plastocyanin
title A QM/MM study of the nature of the entatic state in plastocyanin
title_full A QM/MM study of the nature of the entatic state in plastocyanin
title_fullStr A QM/MM study of the nature of the entatic state in plastocyanin
title_full_unstemmed A QM/MM study of the nature of the entatic state in plastocyanin
title_short A QM/MM study of the nature of the entatic state in plastocyanin
title_sort qm/mm study of the nature of the entatic state in plastocyanin
topic QM/MM
Electron transfer
Plastocyanin
url https://eprints.nottingham.ac.uk/38564/
https://eprints.nottingham.ac.uk/38564/
https://eprints.nottingham.ac.uk/38564/