Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 608

The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.

The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

Shima, Seigo, Pilak, Oliver, Vogt, Sonja, Schick, Michael, Stagni, Marco S., Meyer-Klaucke, Wolfram, Warkentin, Eberhard, Thauer, Rudolf K., Ermler, Ulrich·2008·Science

Abstract

Biological formation and consumption of molecular hydrogen (H 2 ) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp 2 -hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H 2 activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.

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.1158978

Cites

22 of 22 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 22 references

Cited by

See all 608

Metadata

Authors
Shima, S., Pilak, O., Vogt, S., Schick, M., Stagni, M. S., Meyer-Klaucke, W., Warkentin, E., Thauer, R. K., & Ermler, U.
Venue
Science
Published
2008-07-25
Volume
321
Issue
5888
Pages
572-575
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2039892768
Cited by
608
References
22
FWCI
27.35
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: The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site. https://app.cochat.ai/papers/10.1126/science.1158978
The paper
Shima, S., Pilak, O., Vogt, S., Schick, M., Stagni, M. S., Meyer-Klaucke, W., Warkentin, E., Thauer, R. K., & Ermler, U. (2008). The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site. Science. https://doi.org/10.1126/science.1158978

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.