Linear-scaling time-dependent density-functional theory beyond the Tamm-Dancoff approximation: obtaining efficiency and accuracy with in situ optimised local orbitals
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Accepted version
Author(s)
Zuehlsdorff, TJ
Hine, NDM
Payne, MC
Haynes, PD
Type
Journal Article
Abstract
We present a solution of the full time-dependent density-functional theory (TDDFT) eigenvalue equation in the linear response formalism exhibiting a linear-scaling computational complexity with system size, without relying on the simplifying Tamm-Dancoff approximation (TDA). The implementation relies on representing the occupied and unoccupied subspaces with two different sets of in situ optimised localised functions, yielding a very compact and efficient representation of the transition density matrix of the excitation with the accuracy associated with a systematic basis set. The TDDFT eigenvalue equation is solved using a preconditioned conjugate gradient algorithm that is very memory-efficient. The algorithm is validated on a small test molecule and a good agreement with results obtained from standard quantum chemistry packages is found, with the preconditioner yielding a significant improvement in convergence rates. The method developed in this work is then used to reproduce experimental results of the absorption spectrum of bacteriochlorophyll in an organic solvent, where it is demonstrated that the TDA fails to reproduce the main features of the low energy spectrum, while the full TDDFT equation yields results in good qualitative agreement with experimental data. Furthermore, the need for explicitly including parts of the solvent into the TDDFT calculations is highlighted, making the treatment of large system sizes necessary that are well within reach of the capabilities of the algorithm introduced here. Finally, the linear-scaling properties of the algorithm are demonstrated by computing the lowest excitation energy of bacteriochlorophyll in solution. The largest systems considered in this work are of the same order of magnitude as a variety of widely studied pigment-protein complexes, opening up the possibility of studying their properties without having to resort to any semiclassical approximations to parts of the protein environment.
Date Issued
2015-11-28
Date Acceptance
2015-10-29
Citation
Journal of Chemical Physics, 2015, 143 (20), pp.1-13
ISSN
0021-9606
Publisher
American Institute of Physics
Start Page
1
End Page
13
Journal / Book Title
Journal of Chemical Physics
Volume
143
Issue
20
Copyright Statement
© 2015 AIP Publishing LLC. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics. The following article appeared in J. Chem. Phys. 143, 204107 (2015) and may be found at https://dx.doi.org/10.1063/1.4936280
Sponsor
Engineering and Physical Sciences Research Council
Engineering & Physical Science Research Council (EPSRC)
Identifier
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000366319700009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
Grant Number
EP/G036888/1
EP/J015059/1
Subjects
Science & Technology
Physical Sciences
Chemistry, Physical
Physics, Atomic, Molecular & Chemical
Chemistry
Physics
MATTHEWS-OLSON COMPLEX
ELECTRONIC-STRUCTURE CALCULATIONS
EXCITATION-ENERGIES
STATES
EXCHANGE
SPECTRUM
SOLVENT
SYSTEMS
PROTEIN
MATRIX
Publication Status
Published
Article Number
204107
Date Publish Online
2015-11-30