Evidence map›Paper›PMID 26524296›Full record

ArticleJournal of synchrotron radiation2015

A strenuous experimental journey searching for spectroscopic evidence of a bridging nickel-iron-hydride in [NiFe] hydrogenase.

Hongxin Wang, Yoshitaka Yoda, Hideaki Ogata, Yoshihito Tanaka, Wolfgang Lubitz

Abstract read
In one paragraph

Article in Journal of synchrotron radiation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Magnetic interactions between metal sites in complex enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Frontiers in microbiology · 2018
    Article
  10. Review
  11. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Hongxin WangDepartment of Chemistry, University of California, 1 Cyclotron Road, Davis, CA 95616, USA.
Yoshitaka YodaResearch and Utilization Division, SPring-8/JASRI, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Hideaki OgataMax Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany.
Yoshihito TanakaResearch and Utilization Division, SPring-8/JASRI, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Wolfgang LubitzMax Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany.

Funding

X-Ray Raman and Vibrational Mossbauer of MetalloproteinsR01GM065440 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CRAMER, STEPHEN P. · 2002 to 2025
$7.3M
NIGMS NIH HHS GM-65440NIGMS NIH HHS R01 GM065440
6 · The paper itself

Abstract

Direct spectroscopic evidence for a hydride bridge in the Ni-R form of [NiFe] hydrogenase has been obtained using iron-specific nuclear resonance vibrational spectroscopy (NRVS). The Ni-H-Fe wag mode at 675 cm(-1) is the first spectroscopic evidence for a bridging hydride in Ni-R as well as the first iron-hydride-related NRVS feature observed for a biological system. Although density function theory (DFT) calculation assisted the determination of the Ni-R structure, it did not predict the Ni-H-Fe wag mode at ∼ 675 cm(-1) before NRVS. Instead, the observed Ni-H-Fe mode provided a critical reference for the DFT calculations. While the overall science about Ni-R is presented and discussed elsewhere, this article focuses on the long and strenuous experimental journey to search for and experimentally identify the Ni-H-Fe wag mode in a Ni-R sample. As a methodology, the results presented here will go beyond Ni-R and hydrogenase research and will also be of interest to other scientists who use synchrotron radiation for measuring dilute samples or weak spectroscopic features.

Indexed as

Models, ChemicalBinding SitesComputer SimulationEnzyme ActivationHydrogenHydrogenaseHydrogen BondingMagnetic Resonance SpectroscopyProtein BindingHydrogenHydrogenasenickel-iron hydrogenaseiron hydride[NiFe] hydrogenaseNi–H–Fe wag modeNi–RNRVSnuclear resonance vibrational spectroscopyultra-weak signal

Identifiers

PMID26524296
PMCPMC4629863

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.