Evidence map›Paper›PMID 30609080›Full record

ArticleProtein science : a publication of the Protein Society2019

New assay method based on Raman spectroscopy for enzymes reacting with gaseous substrates.

Yuka Kawahara-Nakagawa, Koji Nishikawa, Satoru Nakashima, Shota Inoue, Takehiro Ohta, Takashi Ogura, Yasuteru Shigeta, Katsuyuki Fukutani, Tatsuhiko Yagi, Yoshiki Higuchi

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 48% of its field
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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. Article
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

10 authors at 7 institutions in 1 country.

Yuka Kawahara-NakagawaDepartment of Picobiology, Graduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
Koji NishikawaDepartment of Picobiology, Graduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
Satoru NakashimaDivision for Research Strategy, Institute for Research Initiatives, Nara Institute of Science and Technology, Nara, 630-0192, Japan.
Shota InoueDepartment of Picobiology, Graduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
Takehiro OhtaDepartment of Applied Chemistry, Faculty of Engineering, Sanyo-Onoda City University, Yamaguchi, 756-0884, Japan.
Takashi OguraDepartment of Picobiology, Graduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
Yasuteru ShigetaDivision of Life Science, Center for Computational Science, University of Tsukuba, Ibaraki, 305-8571, Japan.
Katsuyuki FukutaniDepartment of Fundamental Engineering, Institute of Industrial Science, The University of Tokyo, Tokyo, 153-8505, Japan.
Tatsuhiko YagiShizuoka University, Shizuoka, 422-8529, Japan.
Yoshiki HiguchiDepartment of Picobiology, Graduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
University of Hyogo · JPJapan Science and Technology Agency · JPNara Institute of Science and Technology · JPSanyo-Onoda City University · JPShizuoka University · JPThe University of Tokyo · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme activity is typically assayed by quantitatively measuring the initial and final concentrations of the substrates and/or products over a defined time period. For enzymatic reactions involving gaseous substrates, the substrate concentrations can be estimated either directly by gas chromatography or mass spectrometry, or indirectly by absorption spectroscopy, if the catalytic reactions involve electron transfer with electron mediators that exhibit redox-dependent spectral changes. We have developed a new assay system for measuring the time course of enzymatic reactions involving gaseous substrates based on Raman spectroscopy. This system permits continuous monitoring of the gas composition in the reaction cuvette in a non-invasive manner over a prolonged time period. We have applied this system to the kinetic study of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. This enzyme physiologically catalyzes the reversible oxidation of H

Indexed as

CatalysisCatalytic DomainDesulfovibrio vulgarisEnzyme AssaysGasesHydrogenHydrogenaseSpectrum Analysis, RamanGasesHydrogenHydrogenasenickel-iron hydrogenaseH/D exchange reactionkinetic experiment[NiFe] hydrogenasenon-invasive measurementquantitative analysis of gaseous substratesRaman spectroscopy

Identifiers

PMID30609080
PMCPMC6371215
OpenAlexW2907613143

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.