Evidence map›Paper›PMID 34296507›Full record

ArticleChembiochem : a European journal of chemical biology2021

Enzymatic Asymmetric Reduction of Unfunctionalized C=C Bonds with Archaeal Geranylgeranyl Reductases.

Richard Cervinka, Daniel Becker, Steffen Lüdeke, Sonja-Verena Albers, Thomas Netscher, Michael Müller

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 15 citations in OpenAlex.

  1. Asymmetric Reduction of Unactivated Alkenes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
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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

6 authors at 2 institutions in 2 countries.

Richard CervinkaInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104, Freiburg, Germany.
Daniel BeckerInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104, Freiburg, Germany.
Steffen LüdekeInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104, Freiburg, Germany.
Sonja-Verena AlbersInstitute for Biology II, Molecular Biology of Archaea, Faculty of Biology, Albert-Ludwigs-Universität Freiburg, 79104, Freiburg, Germany.
Thomas NetscherResearch and Development, DSM Nutritional Products Ltd., P.O. Box 2676, 4002, Basel, Switzerland.ORCID 0000-0002-9362-3244
Michael MüllerInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104, Freiburg, Germany.ORCID 0000-0002-2742-4992
University of Freiburg · DEDSM (Netherlands) · NL

Funding

Albert-Ludwigs-Universität Freiburg
6 · The paper itself

Abstract

The asymmetric reduction of activated C=C bonds such as enones is well established for non-enzymatic methods as well as in biocatalysis. However, the asymmetric reduction of unfunctionalized C=C bonds is mainly performed with transition metal catalysts whereas biocatalytic approaches are lacking. We have tested two FAD-dependent archaeal geranylgeranyl reductases (GGR) for the asymmetric reduction of isolated C=C bonds. The reduction of up to four double bonds in terpene chains with different chain lengths and head groups was confirmed. Methyl-branched E-alkenes were chemoselectively reduced in the presence of cyclic, terminal or activated alkenes. Using a removable succinate "spacer", farnesol and geraniol could be quantitatively reduced (>99 %). The reduction is strictly (R)-selective (enantiomeric excess >99 %). Hence, GGRs are promising biocatalysts for the asymmetric reduction of unactivated isolated C=C bonds, opening new opportunities for the synthesis of enantiopure branched alkyl chains.

Indexed as

BiocatalysisOxidation-ReductionOxidoreductasesAlkenesArchaeaStereoisomerismTerpenesAlkenesgeranylgeranyl reductaseOxidoreductasesTerpenesasymmetric catalysisasymmetric hydrogenationflavin adenine dinucleotidelipidsoxidoreductases

Identifiers

PMID34296507
PMCPMC8457153
OpenAlexW3184879376

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.