Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins

Research output: Contribution to journalJournal articleResearchpeer-review

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Photosynthetic fuel for heterologous enzymes : the role of electron carrier proteins. / Mellor, Silas Busck; Vavitsas, Konstantinos; Nielsen, Agnieszka Janina Zygadlo; Jensen, Poul Erik.

In: Photosynthesis Research, Vol. 134, No. 3, 2017, p. 329-342.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Mellor, SB, Vavitsas, K, Nielsen, AJZ & Jensen, PE 2017, 'Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins', Photosynthesis Research, vol. 134, no. 3, pp. 329-342. https://doi.org/10.1007/s11120-017-0364-0

APA

Mellor, S. B., Vavitsas, K., Nielsen, A. J. Z., & Jensen, P. E. (2017). Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins. Photosynthesis Research, 134(3), 329-342. https://doi.org/10.1007/s11120-017-0364-0

Vancouver

Mellor SB, Vavitsas K, Nielsen AJZ, Jensen PE. Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins. Photosynthesis Research. 2017;134(3):329-342. https://doi.org/10.1007/s11120-017-0364-0

Author

Mellor, Silas Busck ; Vavitsas, Konstantinos ; Nielsen, Agnieszka Janina Zygadlo ; Jensen, Poul Erik. / Photosynthetic fuel for heterologous enzymes : the role of electron carrier proteins. In: Photosynthesis Research. 2017 ; Vol. 134, No. 3. pp. 329-342.

Bibtex

@article{9ad5ecdb4fae4023b59c4a5fc7bff1e0,
title = "Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins",
abstract = "Plants, cyanobacteria, and algae generate a surplus of redox power through photosynthesis, which makes them attractive for biotechnological exploitations. While central metabolism consumes most of the energy, pathways introduced through metabolic engineering can also tap into this source of reducing power. Recent work on the metabolic engineering of photosynthetic organisms has shown that the electron carriers such as ferredoxin and flavodoxin can be used to couple heterologous enzymes to photosynthetic reducing power. Because these proteins have a plethora of interaction partners and rely on electrostatically steered complex formation, they form productive electron transfer complexes with non-native enzymes. A handful of examples demonstrate channeling of photosynthetic electrons to drive the activity of heterologous enzymes, and these focus mainly on hydrogenases and cytochrome P450s. However, competition from native pathways and inefficient electron transfer rates present major obstacles, which limit the productivity of heterologous reactions coupled to photosynthesis. We discuss specific approaches to address these bottlenecks and ensure high productivity of such enzymes in a photosynthetic context.",
keywords = "Journal Article, Review",
author = "Mellor, {Silas Busck} and Konstantinos Vavitsas and Nielsen, {Agnieszka Janina Zygadlo} and Jensen, {Poul Erik}",
year = "2017",
doi = "10.1007/s11120-017-0364-0",
language = "English",
volume = "134",
pages = "329--342",
journal = "Photosynthesis Research",
issn = "0166-8595",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - Photosynthetic fuel for heterologous enzymes

T2 - the role of electron carrier proteins

AU - Mellor, Silas Busck

AU - Vavitsas, Konstantinos

AU - Nielsen, Agnieszka Janina Zygadlo

AU - Jensen, Poul Erik

PY - 2017

Y1 - 2017

N2 - Plants, cyanobacteria, and algae generate a surplus of redox power through photosynthesis, which makes them attractive for biotechnological exploitations. While central metabolism consumes most of the energy, pathways introduced through metabolic engineering can also tap into this source of reducing power. Recent work on the metabolic engineering of photosynthetic organisms has shown that the electron carriers such as ferredoxin and flavodoxin can be used to couple heterologous enzymes to photosynthetic reducing power. Because these proteins have a plethora of interaction partners and rely on electrostatically steered complex formation, they form productive electron transfer complexes with non-native enzymes. A handful of examples demonstrate channeling of photosynthetic electrons to drive the activity of heterologous enzymes, and these focus mainly on hydrogenases and cytochrome P450s. However, competition from native pathways and inefficient electron transfer rates present major obstacles, which limit the productivity of heterologous reactions coupled to photosynthesis. We discuss specific approaches to address these bottlenecks and ensure high productivity of such enzymes in a photosynthetic context.

AB - Plants, cyanobacteria, and algae generate a surplus of redox power through photosynthesis, which makes them attractive for biotechnological exploitations. While central metabolism consumes most of the energy, pathways introduced through metabolic engineering can also tap into this source of reducing power. Recent work on the metabolic engineering of photosynthetic organisms has shown that the electron carriers such as ferredoxin and flavodoxin can be used to couple heterologous enzymes to photosynthetic reducing power. Because these proteins have a plethora of interaction partners and rely on electrostatically steered complex formation, they form productive electron transfer complexes with non-native enzymes. A handful of examples demonstrate channeling of photosynthetic electrons to drive the activity of heterologous enzymes, and these focus mainly on hydrogenases and cytochrome P450s. However, competition from native pathways and inefficient electron transfer rates present major obstacles, which limit the productivity of heterologous reactions coupled to photosynthesis. We discuss specific approaches to address these bottlenecks and ensure high productivity of such enzymes in a photosynthetic context.

KW - Journal Article

KW - Review

U2 - 10.1007/s11120-017-0364-0

DO - 10.1007/s11120-017-0364-0

M3 - Journal article

C2 - 28285375

VL - 134

SP - 329

EP - 342

JO - Photosynthesis Research

JF - Photosynthesis Research

SN - 0166-8595

IS - 3

ER -

ID: 174273252