2018/02/27 by J.U. Mondal, Barry D. Bruce · 1 voice · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Energy · #Metal-Catalyzed Oxygenation Mechanisms #Metalloenzymes and iron-sulfur proteins #Photosynthetic Processes and Mechanisms
paper · doi:10.1007/s11099-018-0793-9
openalex publication_date 2018/02/27 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
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.