Structural model and excitonic properties of the dimeric RC-LH1-PufX complex from Rhodobacter sphaeroides

Melih Şener; Jen Hsin; Leonardo G. Trabuco; Elizabeth Villa; Pu Qian; C. Neil Hunter; Klaus Schulten

doi:10.1016/j.chemphys.2009.01.003

Structural model and excitonic properties of the dimeric RC-LH1-PufX complex from Rhodobacter sphaeroides

Melih Şener, Jen Hsin, Leonardo G. Trabuco, Elizabeth Villa, Pu Qian, C. Neil Hunter, Klaus Schulten

Physics

Research output: Contribution to journal › Article › peer-review

Abstract

The light-harvesting apparatus of the purple bacterial photosynthetic unit consists of a pool of peripheral light-harvesting complexes that transfer excitation energy to a reaction center (RC) via the surrounding pigment-protein complex LH1. Recent electron microscopy and atomic force microscopy studies have revealed that RC-LH1 units of Rhodobacter (Rba.) sphaeroides form membrane-bending dimeric complexes together with the polypeptide PufX. We present a structural model for these RC-LH1-PufX dimeric complexes constructed using the molecular dynamics flexible fitting method based on an EM density map. The arrangement of the LH1 BChls displays a distortion near the proposed location of the PufX polypeptide. The resulting atomic model for BChl arrays is used to compute the excitonic properties of the dimeric RC-LH1 complex. A comparison is presented between the structural and excitonic features of the S-shaped dimeric BChl array of Rba. sphaeroides and the circular BChl arrangement found in other purple bacteria.

Original language	English (US)
Pages (from-to)	188-197
Number of pages	10
Journal	Chemical Physics
Volume	357
Issue number	1-3
DOIs	https://doi.org/10.1016/j.chemphys.2009.01.003
State	Published - Feb 23 2009

Keywords

Excitons
Membrane curvature
Molecular dynamics/flexible fitting
Photosynthesis
Purple bacteria
Reaction center

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Physics and Astronomy(all)

Access to Document

10.1016/j.chemphys.2009.01.003

Fingerprint Dive into the research topics of 'Structural model and excitonic properties of the dimeric RC-LH1-PufX complex from Rhodobacter sphaeroides'. Together they form a unique fingerprint.

Cite this

@article{ea2f5be610c046189517b3eb798d0b4e,

title = "Structural model and excitonic properties of the dimeric RC-LH1-PufX complex from Rhodobacter sphaeroides",

abstract = "The light-harvesting apparatus of the purple bacterial photosynthetic unit consists of a pool of peripheral light-harvesting complexes that transfer excitation energy to a reaction center (RC) via the surrounding pigment-protein complex LH1. Recent electron microscopy and atomic force microscopy studies have revealed that RC-LH1 units of Rhodobacter (Rba.) sphaeroides form membrane-bending dimeric complexes together with the polypeptide PufX. We present a structural model for these RC-LH1-PufX dimeric complexes constructed using the molecular dynamics flexible fitting method based on an EM density map. The arrangement of the LH1 BChls displays a distortion near the proposed location of the PufX polypeptide. The resulting atomic model for BChl arrays is used to compute the excitonic properties of the dimeric RC-LH1 complex. A comparison is presented between the structural and excitonic features of the S-shaped dimeric BChl array of Rba. sphaeroides and the circular BChl arrangement found in other purple bacteria.",

keywords = "Excitons, Membrane curvature, Molecular dynamics/flexible fitting, Photosynthesis, Purple bacteria, Reaction center",

author = "Melih {\c S}ener and Jen Hsin and Trabuco, {Leonardo G.} and Elizabeth Villa and Pu Qian and Hunter, {C. Neil} and Klaus Schulten",

note = "Funding Information: The authors would like to thank D. Chandler, J. Gumbart, C.B. Harrison, P.A. Bullough, and R. van Grondelle for useful discussions. This work was supported by National Science Foundation grant MCB0744057 and National Institutes of Health grant P41-RR05969 (to K.S.) as well as the Biotechnology and Biological Research Council, UK (grant to C.N.H.). Computer time was provided at the National Center for Supercomputing Applications and the Texas Advanced Computing Center via a NSF Large Resources Allocation Committee grant MCA93S028. Molecular images in this paper were generated with VMD [118] . ",

year = "2009",

month = feb,

day = "23",

doi = "10.1016/j.chemphys.2009.01.003",

language = "English (US)",

volume = "357",

pages = "188--197",

journal = "Chemical Physics",

issn = "0301-0104",

publisher = "Elsevier",

number = "1-3",

}

TY - JOUR

T1 - Structural model and excitonic properties of the dimeric RC-LH1-PufX complex from Rhodobacter sphaeroides

AU - Şener, Melih

AU - Hsin, Jen

AU - Trabuco, Leonardo G.

AU - Villa, Elizabeth

AU - Qian, Pu

AU - Hunter, C. Neil

AU - Schulten, Klaus

N1 - Funding Information: The authors would like to thank D. Chandler, J. Gumbart, C.B. Harrison, P.A. Bullough, and R. van Grondelle for useful discussions. This work was supported by National Science Foundation grant MCB0744057 and National Institutes of Health grant P41-RR05969 (to K.S.) as well as the Biotechnology and Biological Research Council, UK (grant to C.N.H.). Computer time was provided at the National Center for Supercomputing Applications and the Texas Advanced Computing Center via a NSF Large Resources Allocation Committee grant MCA93S028. Molecular images in this paper were generated with VMD [118] .

PY - 2009/2/23

Y1 - 2009/2/23

N2 - The light-harvesting apparatus of the purple bacterial photosynthetic unit consists of a pool of peripheral light-harvesting complexes that transfer excitation energy to a reaction center (RC) via the surrounding pigment-protein complex LH1. Recent electron microscopy and atomic force microscopy studies have revealed that RC-LH1 units of Rhodobacter (Rba.) sphaeroides form membrane-bending dimeric complexes together with the polypeptide PufX. We present a structural model for these RC-LH1-PufX dimeric complexes constructed using the molecular dynamics flexible fitting method based on an EM density map. The arrangement of the LH1 BChls displays a distortion near the proposed location of the PufX polypeptide. The resulting atomic model for BChl arrays is used to compute the excitonic properties of the dimeric RC-LH1 complex. A comparison is presented between the structural and excitonic features of the S-shaped dimeric BChl array of Rba. sphaeroides and the circular BChl arrangement found in other purple bacteria.

AB - The light-harvesting apparatus of the purple bacterial photosynthetic unit consists of a pool of peripheral light-harvesting complexes that transfer excitation energy to a reaction center (RC) via the surrounding pigment-protein complex LH1. Recent electron microscopy and atomic force microscopy studies have revealed that RC-LH1 units of Rhodobacter (Rba.) sphaeroides form membrane-bending dimeric complexes together with the polypeptide PufX. We present a structural model for these RC-LH1-PufX dimeric complexes constructed using the molecular dynamics flexible fitting method based on an EM density map. The arrangement of the LH1 BChls displays a distortion near the proposed location of the PufX polypeptide. The resulting atomic model for BChl arrays is used to compute the excitonic properties of the dimeric RC-LH1 complex. A comparison is presented between the structural and excitonic features of the S-shaped dimeric BChl array of Rba. sphaeroides and the circular BChl arrangement found in other purple bacteria.

KW - Excitons

KW - Membrane curvature

KW - Molecular dynamics/flexible fitting

KW - Photosynthesis

KW - Purple bacteria

KW - Reaction center

UR - http://www.scopus.com/inward/record.url?scp=59649084842&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=59649084842&partnerID=8YFLogxK

U2 - 10.1016/j.chemphys.2009.01.003

DO - 10.1016/j.chemphys.2009.01.003

M3 - Article

C2 - 20161332

AN - SCOPUS:59649084842

VL - 357

SP - 188

EP - 197

JO - Chemical Physics

JF - Chemical Physics

SN - 0301-0104

IS - 1-3

ER -