Chauvet, A., Jagannathan, B., Golbeck, J.H. et al. (1 more author) (2009) Type I reaction center from the green sulfur bacterium Chlorobium tepidum: is Chl a a primary electron acceptor? Biophysical Journal, 96 (3). Supplement 1. 526a-527a. ISSN 0006-3495
Abstract
The green sulfur bacterium Chlorobium tepidum has one of the simplest type I reaction center (RC) complexes. While its structure is still unknown, biochemical and protein sequence analyses suggest that it is similar to photosystem I (PS I), with two BChl a forming a special pair P840, four Chl a serving as pairs of accessory and primary electron acceptor (A0) pigments and 14 BChl a constituting as an immediate RC antenna. This is a dramatic simplification compared to PS I RC, where 90 Chl a antenna pigments serve as antenna and 6 additional Chl a molecules function as electron transfer cofactors. The resulting spectral congestion has prevented direct visualization of ultrafast electron transfer processes within PS I RC and even the sequence of primary electron transfer processes in PS I is still under debate. The suggested presence of two types of pigments in RC from Chlorobium tepidum removes spectral congestion and opens a way to directly visualize electron transfer steps in type I RC using ultrafast spectroscopy, since the Chl a and BChl a pigments absorb at ∼670 nm and ∼800 nm, respectively. To confirm the proposed functional role of Chl a as electron transfer cofactor we performed extensive ultrafast optical pump-probe experiments on different preparations of RC complexes from Chlorobium tepidum, revealing energy/electron transfer rates between different groups of pigments. Surprisingly, we found that ∼3 out of 4 Chl a pigments do not transfer excitation energy to the BChl a antenna or to P840, which indicates that these pigments must be >20Å away from any other BChl a pigment and thus argues against the suggested presence of 4 Chl a in the reaction center core complex.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2009 Biophysical Society. Published by Elsevier Inc. |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 14 Jul 2017 10:35 |
Last Modified: | 14 Jul 2017 10:35 |
Published Version: | https://doi.org/10.1016/j.bpj.2008.12.2717 |
Status: | Published |
Publisher: | Elsevier |
Refereed: | Yes |
Identification Number: | 10.1016/j.bpj.2008.12.2717 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:108918 |