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Journal Article

Asymmetric hydrogen-bonding of the quinone cofactor in photosystem I probed by 13C-labeled naphthoquinones

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Zimmermann,  Herbert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Pushkar, Y. N., Golbeck, J. H., Stehlik, D., & Zimmermann, H. (2004). Asymmetric hydrogen-bonding of the quinone cofactor in photosystem I probed by 13C-labeled naphthoquinones. The Journal of Physical Chemistry B, 108(27), 9439-9448. doi:10.1021/jp0361879.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-3409-8
Abstract
In photosystem I (PS I) the phylloquinone secondary acceptor functions as a one electron gate similar to the QA quinone secondary acceptor in type II reaction centers. The quinone radical anion formed during charge separation as part of the P700+• A1-• radical pair state is known to have a highly asymmetric electron spin density distribution, which is attributed to asymmetric hydrogen bonding with the protein environment. Here, the native phylloquinone is replaced by specifically 13C-labeled 2-methyl-1,4-naphthoquinones (2-methyl-4-13C-1,4-naphthoquinone and 2-13C-methyl-1,4-naphthoquinone) to probe the spin density distribution in two relevant quinone ring positions. The menB phylloquinone biosynthetic pathway mutant was used because it allows for efficient in vitro quinone replacement in isolated PS I trimers. X- and Q-band time-resolved EPR spectroscopy was used to determine the 13C hyperfine tensors in the functional P700+• A1-• state. For 2-methyl-4-13C-1,4-naphthoquinone anion radical the largest hyperfine tensor component Azz = 44 MHz was found to be considerably larger than those determined in bacterial reaction centers. The PS I structure at 2.5 Å resolution shows a single H-bond from the backbone NH group of a specific leucine residue. Such a highly asymmetric H-bonding is confirmed here for the functional P700+• A1-•state. Experimental evidence for an unusual backbone H-bond strength is analyzed by comparing the quinone binding site with that in bacterial reaction centers and possible mechanisms of increased H-bond strength are considered.