Evidence map›Paper›PMID 33783938›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.

Christian Lorent, Vladimir Pelmenschikov, Stefan Frielingsdorf, Janna Schoknecht, Giorgio Caserta, Yoshitaka Yoda, Hongxin Wang, Kenji Tamasaku, Oliver Lenz, Stephen P Cramer and 3 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
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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

13 authors.

Christian LorentDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0001-9057-4523
Vladimir PelmenschikovDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0002-0523-4418
Stefan FrielingsdorfDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0002-4141-7836
Janna SchoknechtDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0002-2896-8174
Giorgio CasertaDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0003-0986-3059
Yoshitaka YodaJapan Synchrotron Radiation Research Institute, SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo, 679-5198, Japan.ORCID 0000-0003-3062-8651
Hongxin WangSETI Institute, 189 Bernardo Avenue, Mountain View, California, 94043, USA.ORCID 0000-0002-7325-0161
Kenji TamasakuRIKEN SPring-8 center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.ORCID 0000-0003-1440-0518
Oliver LenzDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0003-4550-5128
Stephen P CramerSETI Institute, 189 Bernardo Avenue, Mountain View, California, 94043, USA.ORCID 0000-0002-3751-7623
Marius HorchDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0001-6656-1749
Lars LauterbachDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0002-6601-6473
Ingo ZebgerDepartment of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623, Berlin, Germany.ORCID 0000-0002-6354-3585

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 R01 GM065440NIH HHS GM-65440
6 · The paper itself

Abstract

To study metalloenzymes in detail, we developed a new experimental setup allowing the controlled preparation of catalytic intermediates for characterization by various spectroscopic techniques. The in situ monitoring of redox transitions by infrared spectroscopy in enzyme lyophilizate, crystals, and solution during gas exchange in a wide temperature range can be accomplished as well. Two O

Indexed as

HydrogenaseOxidation-ReductionCrystallography, X-RayDensity Functional TheoryFreeze DryingModels, MolecularSpectrum Analysis, RamanHydrogenasenickel-iron hydrogenasebiocatalysisin situ spectroscopymetalloenzymes[NiFe]-hydrogenasevibrational spectroscopy

Identifiers

PMID33783938
PMCPMC8360142

What OpenQuestion holds

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Registered trials

None linked

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.