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          Institute: MPI für medizinische Forschung     Collection: Arbeitsgruppe Zimmermann     Display Documents

ID: 569176.0, MPI für medizinische Forschung / Arbeitsgruppe Zimmermann
Single−Sided Hydrogen Bonding to the Quinone Cofactor in Photosystem I Probed by Selective 13C−Labelled Naphthoquinones and Transient EPR
Translation of Title:Single−Sided Hydrogen Bonding to the Quinone Cofactor in Photosystem I Probed by Selective 13C−Labelled Naphthoquinones and Transient EPR
Authors:Karyagina, I.; Golbeck, John H.; Srinivasan, N.; Stehlik, Dietmar; Zimmermann, Herbert
Date of Publication (YYYY-MM-DD):2006-01-01
Title of Journal:Appl. Magn. Reson.
Journal Abbrev.:Appl. Magn. Reson.
Issue / Number:3
Start Page:287
End Page:310
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Hydrogen bonding between the protein and one or both of the two 1,4−quinone carbonyl groups of a benzo− or naphtho−quinone constitutes a significant protein cofactor interaction in photosynthetic reaction centers. The redistribution of charge and spin density due to a particular H−bonding scheme leaves the largest hyperfine couplings (hfc) at the highest density positions, i.e., the nuclei of the carbonyl groups directly involved in H−bonding. The spin density changes at the ring carbon positions are accessed experimentally via electron paramagnetic resonance−determined hfc tensor elements of selective 13C isotope labels in one of the two carbonyl groups. Complete hfc tensor data are presented for each of the 13C positions in the functional charge−separated state in reaction centers of photosystem I (PS I) isolated from cyanobacteria. A highly asymmetric H−bonding scheme for the A1 quinone binding site due to a single dominant H−bond to one carbonyl group is confirmed. A comparison to other well−studied quinone binding sites of other protein−cofactor systems with more complex H−bonding schemes reveals the uniqueness of the PS I site. The single−sided A1 quinone site provides an ideal test case for the various sets of density functional theory (DFT) calculations that are currently available. While the overall agreement between experimental and calculated data is quite satisfactory, a significant discrepancy is found for the high−spin−density 13C position associated with the H−bonded carbonyl. The dominant hfc component (and spin density) is underestimated in the DFT calculations, not only for the high−asymmetry case in PS I, but also for other quinone binding sites with less asymmetry that result from more complex H−bonding schemes. The consequences and potential relevance of this finding for biological function are discussed
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Arbeitsgruppe Zimmermann
MPI für medizinische Forschung/Abteilung Molekulare Physik
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