Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 751

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure of the Cytochrome b 6 f Complex of Oxygenic Photosynthesis: Tuning the Cavity

Kurisu, Genji, Zhang, Huamin, Smith, Janet L., Cramer, William A.·2003·Science

Abstract

The cytochrome b 6 f complex provides the electronic connection between the photosystem I and photosystem II reaction centers of oxygenic photosynthesis and generates a transmembrane electrochemical proton gradient for adenosine triphosphate synthesis. A 3.0 angstrom crystal structure of the dimeric b 6 f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quinone-analog inhibitor, and a novel heme are bound. The core of the b 6 f complex is similar to the analogous respiratory cytochrome bc 1 complex, but the domain arrangement outside the core and the complement of prosthetic groups are strikingly different. The motion of the Rieske iron-sulfur protein extrinsic domain, essential for electron transfer, must also be different in the b 6 f complex.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1126/science.1090165

Cites

1 of 1 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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

Cites

Show all 1 references

Cited by

See all 751

Metadata

Authors
Kurisu, G., Zhang, H., Smith, J. L., & Cramer, W. A.
Venue
Science
Published
2003-11-07
Volume
302
Issue
5647
Pages
1009-1014
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2120875291
Cited by
751
References
1
FWCI
17.16
Type
journal article
Language
en
Open access
closed

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: Structure of the Cytochrome b 6 f Complex of Oxygenic Photosynthesis: Tuning the Cavity. https://app.cochat.ai/papers/10.1126/science.1090165
The paper
Kurisu, G., Zhang, H., Smith, J. L., & Cramer, W. A. (2003). Structure of the Cytochrome b 6 f Complex of Oxygenic Photosynthesis: Tuning the Cavity. Science. https://doi.org/10.1126/science.1090165

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.