title: Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced fourier transform infrared difference spectroscopy.
abstract: Fourier transform infrared (FTIR) signals of a histidine side chain were identified in flash-induced S(2)/S(1) difference spectra of the oxygen-evolving complex (OEC) of photosystem II (PS II) using PS II membranes from globally (15)N-labeled spinach and PS II core complexes from Synechocystis cells in which both the imidazole nitrogens of histidine were selectively labeled with (15)N. A negative band at 1113-1114 cm(-1) was downshifted by 7 cm(-1) upon both global (15)N-labeling and selective [(15)N]His labeling, and assigned to the C-N stretching mode of the imidazole ring. This band was unaffected by H-D exchange in the PS II preparations. In addition, several peaks observed at 2500-2850 cm(-1) all downshifted upon global and selective (15)N-labeling. These were ascribed to Fermi resonance peaks on a hydrogen-bonding N-H stretching band of the histidine side chain. FTIR measurements of model compounds of the histidine side chain showed that the C-N stretching band around 1100 cm(-)(1) can be a useful IR marker of the protonation form of the imidazole ring. The band appeared with frequencies in the following order: Npi-protonated (>1100 cm(-1)) > imidazolate > imidazolium > Ntau-protonated (<1095 cm(-1)). The frequency shift upon N-deuteration was occurred in the following order: imidazolium (15-20 cm(-1)) > Ntau-protonated (5-10 cm(-1)) > Npi-protonated approximately imidazolate ( approximately 0 cm(-1)). On the basis of these findings together with the Fermi resonance peaks at >2500 cm(-1) as a marker of N-H hydrogen-bonding, we concluded that the histidine residue in the S(2)/S(1) spectrum is protonated at the Npi site and that this Npi-H is hydrogen bonded. This histidine side chain probably ligated the redox-active Mn ion at the Ntau site, and thus, oxidation of the Mn cluster upon S(2) formation perturbed the histidine vibrations, causing this histidine to appear in the S(2)/S(1) difference spectrum.
authors.affiliation: Photosynthesis Research Laboratory, The Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Noguchi
authors.forename: Y
authors.initials: Y
authors.lastname: Inoue
authors.forename: X S
authors.initials: XS
authors.lastname: Tang
mesh_terms: D000458:Cyanobacteria / Q000737:chemistry; D003903:Deuterium / Q000378:metabolism; D006639:Histidine / Q000302:isolation & purification / Q000378:metabolism*; D006860:Hydrogen Bonding; D008024:Ligands; D008027:Light; D008956:Models, Chemical; D010100:Oxygen / Q000378:metabolism*; D010782:Photolysis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D045332:Photosystem II Protein Complex; D011522:Protons; D017550:Spectroscopy, Fourier Transform Infrared; D018724:Spinacia oleracea / Q000737:chemistry
chemical_list: D008024:Ligands; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D011522:Protons; D006639:Histidine; D003903:Deuterium; D010100:Oxygen