This Article Full Text Full Text (PDF) All Versions of this Article: biophysj.104.058693v1 88/6/4178    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Dashdorj, N. Articles by Savikhin, S. Search for Related Content PubMed PubMed Citation Articles by Dashdorj, N. Articles by Savikhin, S.

The Single Chlorophyll a Molecule in the Cytochrome b₆f Complex: Unusual Optical Properties Protect the Complex against Singlet Oxygen

Naranbaatar Dashdorj ^*, Huamin Zhang , Hanyoup Kim ^*, Jiusheng Yan , William A. Cramer  and Sergei Savikhin ^*

^* Department of Physics and Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907

Correspondence: Address reprint requests to Sergei Savikhin, Tel.: 765 494 3017; Fax: 765-494-0706; E-mail: sergei{at}physics.purdue.edu.

The cytochrome b₆f complex of oxygenic photosynthesis mediates electron transfer between the reaction centers of photosystems I and II and facilitates coupled proton translocation across the membrane. High-resolution x-ray crystallographic structures (Kurisu et al., 2003; Stroebel et al., 2003) of the cytochrome b₆f complex unambiguously show that a Chl a molecule is an intrinsic component of the cytochrome b₆f complex. Although the functional role of this Chl a is presently unclear (Kühlbrandt, 2003), an excited Chl a molecule is known to produce toxic singlet oxygen as the result of energy transfer from the excited triplet state of the Chl a to oxygen molecules. To prevent singlet oxygen formation in light-harvesting complexes, a carotenoid is typically positioned within 4 Å of the Chl a molecule, effectively quenching the triplet excited state of the Chl a. However, in the cytochrome b₆f complex, the ß-carotene is too far (14 Å) from the Chl a for effective quenching of the Chl a triplet excited state. In this study, we propose that in this complex, the protection is at least partly realized through special arrangement of the local protein structure, which shortens the singlet excited state lifetime of the Chl a by a factor of 20–25 and thus significantly reduces the formation of the Chl a triplet state. Based on optical ultrafast absorption difference experiments and structure-based calculations, it is proposed that the Chl a singlet excited state lifetime is shortened due to electron exchange transfer with the nearby tyrosine residue. To our knowledge, this kind of protection mechanism against singlet oxygen has not yet been reported for any other chlorophyll-containing protein complex. It is also reported that the Chl a molecule in the cytochrome b₆f complex does not change orientation in its excited state.

This article has been cited by other articles:

				H. Kim, N. Dashdorj, H. Zhang, J. Yan, W. A. Cramer, and S. Savikhin An Anomalous Distance Dependence of Intraprotein Chlorophyll-Carotenoid Triplet Energy Transfer Biophys. J., October 1, 2005; 89(4): L28 - L30. [Abstract] [Full Text] [PDF]