ArticleBiophysical journal1999
A Difference Fourier transform infrared study of tyrosyl radical Z* decay in photosystem II.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- The Human Circadian Clock Protein Cryptochrome-1 Responds to Photochemistry by Conformational Changes.Journal of the American Chemical Society · 2026Article
- Structure Function Studies of Photosystem II Using X-Ray Free Electron Lasers.Annual review of biophysics · 2024Review
- Time-Resolved Infrared and Visible Spectroscopy on Cryptochrome aCRY: Basis for Red Light Reception.Biophysical journal · 2019Article
- Proton coupled electron transfer and redox-active tyrosine Z in the photosynthetic oxygen-evolving complex.Journal of the American Chemical Society · 2011Article
- Perturbations of aromatic amino acids are associated with iron cluster assembly in ribonucleotide reductase.Journal of the American Chemical Society · 2011Article
- Proton coupled electron transfer and redox active tyrosines in Photosystem II.Journal of photochemistry and photobiology. B, BiologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Photosystem II (PSII) contains a redox-active tyrosine, Z* Difference Fourier transform infrared (FTIR) spectroscopy can be used to obtain structural information about this species, which is a neutral radical, Z*, in the photooxidized form. Previously, we have used isotopic labeling, inhibitors, and site-directed mutagenesis to assign a vibrational line at 1478 cm(-1) to Z*; these studies were performed on highly resolved PSII preparations at pH 7.5, under conditions where Q(A)(-) and Q(B)(-) make no detectable contribution to the vibrational spectrum (Kim, Ayala, Steenhuis, Gonzalez, Razeghifard, and Barry. 1998. Biochim. Biophys. Acta. 1366:330-354). Here, time-resolved infrared data associated with the reduction of tyrosyl radical Z* were acquired from spinach core PSII preparations at pH 6.0. Electron paramagnetic resonance spectroscopy and fluorescence control experiments were employed to measure the rate of Q(A)(-) and Z* decay. Q(B)(-) did not recombine with Z* under these conditions. Difference FTIR spectra, acquired over this time regime, exhibited time-dependent decreases in the amplitude of a 1478 cm(-1) line. Quantitative comparison of the rates of Q(A)(-) and Z* decay with the decay of the 1478 cm(-1) line supported the assignment of a 1478 cm(-1) component to Z*. Comparison with difference FTIR spectra obtained from PSII samples, in which tyrosine is labeled, supported this conclusion and identified other spectral components assignable to Z* and Z. To our knowledge, this is the first kinetic study to use quantitative comparison of kinetic constants in order to assign spectral features to Z*.
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