Ferredoxin: the central hub connecting photosystem I to cellular metabolism

Title:

Ferredoxin: the central hub connecting photosystem I to cellular metabolism

Creator:

Mondal, J. and Bruce, B. D.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:034b7349-31bf-49c6-b794-835bb9c27090
uuid:034b7349-31bf-49c6-b794-835bb9c27090
issn:0300-3604
doi:10.1007/s11099-018-0793-9

Subject:

přenos elektronů, electron transfer, cellular metabolism, ferredoxin, global interaction, oxidation-reduction, 2, and 581

Type:

model:article and TEXT

Format:

print, bez média, and svazek

Description:

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., J. Mondal, B. D. Bruce., and Obsahuje bibliografické odkazy

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

279-293

Source:

Photosynthetica | 2018 Volume:56 | Number:1

Harvested from:

CDK

Metadata only:

false