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Ferredoxin: the central hub connecting photosystem I to cellular metabolism

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Ferredoxin (Fd) is a small soluble iron-sulfur protein essential in almost all oxygenic photosynthetic organisms. It contains a single [2Fe-2S] cluster coordinated by four cysteine ligands. It accepts electrons from the stromal surface of PSI and facilitates transfer to a myriad of acceptors involved in diverse metabolic processes, including generation of NADPH via Fd-NADP-reductase, cyclic electron transport for ATP synthesis, nitrate reduction, nitrite reductase, sulfite reduction, hydrogenase and other reductive reactions. Fd serves as the central hub for these diverse cellular reactions and is integral to complex cellular metabolic networks. We describe advances on the central role of Fd and its evolutionary role from cyanobacteria to algae/plants. We compare structural diversity of Fd partners to understand this orchestrating role and shed light on how Fd dynamically partitions between competing partner proteins to enable the optimum transfer of PSI-derived electrons to support cell growth and metabolism.

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bilin reductases


cyclic electron transfer





Fdred :

reduced Fd

Fdox :

oxidized Fd


flavin adenine dinucleotide


flavin mononucleotide



FNRred :

reduced FNR

FNRox :

oxidized FNR


Fd:Tro reductase


glutamine synthase


glutamate synthase

Kd :

dissociation constant

Ket :

electron transfer rate constant


NADPH dehydrogenase


nitrite reductase


nitrate reductase




3E/3Z phycocyanobilin




3Z/3E phycoerythrobilin


3E/3Z phytochromobilin


root-mean-square deviation


sulfite reductase




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Author information

Correspondence to B. D. Bruce.

Additional information

Acknowledgments: Support to B.D.B. and J.M. has been provided from the Gibson Family Foundation, the Tennessee Plant Research Center, and the Dr. Donald L. Akers Faculty Enrichment Fellowship to B.D.B. and National Science Foundation support to B.D.B. (DGE-0801470 and EPS-1004083). J.M. has also been supported by a seed grant from Institute for Secure and Sustainable Environment, UTK and a donation from the Hallsdale-Powell Utility District. We thank Nathan G. Brady and Alexandra H. Teodor for critically reading the manuscript. We thank Sarah J. Cooper for her immense help in data analysis using the CoCoMaps server. Travel to 7th International Meeting on Sustainable Research in Photosynthesis was provided by the Tennessee Plant Research Center for J. M.

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Mondal, J., Bruce, B.D. Ferredoxin: the central hub connecting photosystem I to cellular metabolism. Photosynthetica 56, 279–293 (2018). https://doi.org/10.1007/s11099-018-0793-9

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Additional key words

  • cellular metabolism
  • electron transfer
  • ferredoxin
  • global interaction
  • oxidation-reduction