Evidence map›Paper›PMID 27119279›Full record

ArticleACS chemical biology2016

Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.

Silas Busck Mellor, Agnieszka Zygadlo Nielsen, Meike Burow, Mohammed Saddik Motawia, Dainius Jakubauskas, Birger Lindberg Møller, Poul Erik Jensen

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  7. Photosynthesis: Genetic Strategies Adopted to Gain Higher Efficiency.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Light-driven biocatalytic oxidation.Chemical science · 2022
    Review
  10. Review
  11. Article
  12. Review
  13. Improved photosynthetic capacity and photosystem I oxidation via heterologous metabolism engineering in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  17. 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

7 authors at 1 institution in 1 country.

Silas Busck MellorCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Agnieszka Zygadlo NielsenCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Meike BurowCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Mohammed Saddik MotawiaCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Dainius JakubauskasCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Birger Lindberg MøllerCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
Poul Erik JensenCopenhagen Plant Science Center, Department of Plant and Environmental Sciences, University of Copenhagen , Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark.
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450s (P450s) are key enzymes in the synthesis of bioactive natural products in plants. Efforts to harness these enzymes for in vitro and whole-cell production of natural products have been hampered by difficulties in expressing them heterologously in their active form, and their requirement for NADPH as a source of reducing power. We recently demonstrated targeting and insertion of plant P450s into the photosynthetic membrane and photosynthesis-driven, NADPH-independent P450 catalytic activity mediated by the electron carrier protein ferredoxin. Here, we report the fusion of ferredoxin with P450 CYP79A1 from the model plant Sorghum bicolor, which catalyzes the initial step in the pathway leading to biosynthesis of the cyanogenic glucoside dhurrin. Fusion with ferredoxin allows CYP79A1 to obtain electrons for catalysis by interacting directly with photosystem I. Furthermore, electrons captured by the fused ferredoxin moiety are directed more effectively toward P450 catalytic activity, making the fusion better able to compete with endogenous electron sinks coupled to metabolic pathways. The P450-ferredoxin fusion enzyme obtains reducing power solely from its fused ferredoxin and outperforms unfused CYP79A1 in vivo. This demonstrates greatly enhanced electron transfer from photosystem I to CYP79A1 as a consequence of the fusion. The fusion strategy reported here therefore forms the basis for enhanced partitioning of photosynthetic reducing power toward P450-dependent biosynthesis of important natural products.

Indexed as

LightBiological ProductsCytochrome P-450 Enzyme SystemFerredoxinsNicotianaOsmolar ConcentrationBiological ProductsCytochrome P-450 Enzyme SystemFerredoxins

Identifiers

PMID27119279
PMCPMC4949584
OpenAlexW2344094488

What OpenQuestion holds

Textmetadata
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.