The DOI matches its Crossref record.
Proximity of the manganese cluster of photosystem II to the redox-active tyrosine YZ.
Open accessAbstract
Electron spin echo electron-nuclear double resonance (ESE-ENDOR) experiments performed on a broad radical electron paramagnetic resonance (EPR) signal observed in photosystem II particles depleted of Ca2+ indicate that this signal arises from the redox-active tyrosine YZ. The tyrosine EPR signal width is increased relative to that observed in a manganese-depleted preparation due to a magnetic interaction between the photosystem II manganese cluster and the tyrosine radical. The manganese cluster is located asymmetrically with respect to the symmetry-related tyrosines YZ and YD. The distance between the YZ tyrosine and the manganese cluster is estimated to be approximately 4.5 A. Due to this close proximity of the Mn cluster and the redox-active tyrosine YZ, we propose that this tyrosine abstracts protons from substrate water bound to the Mn cluster.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659
Protein Radicals in Enzyme Catalysis
Stubbe, J., & van der Donk, W. A. (1998) · Chemical Reviews · doi:10.1021/cr9400875 · Cited by 1,377
Oxygen Production in Nature: A Light-Driven Metalloradical Enzyme Process
Tommos, C., & Babcock, G. T. (1998) · Accounts of Chemical Research · doi:10.1021/ar9600188 · Cited by 406
Metadata
- Authors
- Gilchrist, M. L., Ball, J. A., Randall, D. W., & Britt, R. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-10-10
- Volume
- 92
- Issue
- 21
- Pages
- 9545-9549
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2147121758
- Cited by
- 200
- References
- 0
- FWCI
- 7.22
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Proximity of the manganese cluster of photosystem II to the redox-active tyrosine YZ. https://app.cochat.ai/papers/10.1073/pnas.92.21.9545
- The paper
- Gilchrist, M. L., Ball, J. A., Randall, D. W., & Britt, R. D. (1995). Proximity of the manganese cluster of photosystem II to the redox-active tyrosine YZ. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.21.9545
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
