A difference Fourier-transform infrared study of two redox-active tyrosine residues in photosystem II.
Photosystem II, the photosynthetic water-oxidizing complex, contains two redox-active tyrosine residues. Although current models suggest that these tyrosines are located in symmetric positions in the reaction center, there are functional differences between them. To elucidate those structural factors that give rise to this functional asymmetry, we have used difference Fourier-transform infrared spectroscopy to obtain the vibrational difference spectrum associated with the oxidation of each of these redox-active residues. Isotopic labeling was employed to definitively assign vibrational lines to the redox-active tyrosines. This work has shown that the vibrational spectra of the two redox-active species are significantly different from each other. This result suggests that the structure of the redox-active residue helps to determine its role in electron transfer in the reaction center.
MacDonald
G M
GM
Department of Biochemistry, University of Minnesota, St. Paul 55108.
Bixby
K A
KA
Barry
B A
BA
D000458:Cyanobacteria / Q000737:chemistry / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D008345:Manganese / Q000737:chemistry; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D045332:Photosystem II Protein Complex; D017550:Spectroscopy, Fourier Transform Infrared; D014443:Tyrosine / Q000737:chemistry*
D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D014443:Tyrosine; D008345:Manganese