Recombinant Coffea arabica Cytochrome b6-f complex subunit 4 (petD) is a protein expressed in E. coli, fused with an N-terminal His tag, and derived from Coffea arabica (Arabian coffee) . It is a full-length protein consisting of 160 amino acids . Cytochrome b6-f complex subunit 4 (petD) is a component of the cytochrome b6-f complex, essential for photosynthetic electron transport in plants and cyanobacteria .
The cytochrome $$b_6f $$ complex is a hetero-oligomeric membrane protein complex critical in the electron transport chain of oxygenic photosynthesis . It mediates electron transport between Photosystem II (PSII) and Photosystem I (PSI) . The complex facilitates plastoquinol-plastocyanin oxidoreductase activity, linear and PSI cyclic electron flow, proton translocation across the membrane, and photosynthetic redox control of energy distribution .
In flowering plants, the cytochrome $$b_6f $$ complex comprises at least nine subunits and exists as a dimer . These subunits are encoded by both nuclear and plastid genes . The complex includes subunits such as PetA (cytochrome f), PetB (cytochrome $$b_6$$), and PetD (subunit IV) . PetD is homologous to the C-terminal half of the cytochrome b subunit found in $$bc_1$$ complexes .
The cytochrome $$b_6f $$ complex from M. laminosus consists of eight polypeptide subunits: PetA (cytochrome f), PetB (cytochrome $$b_6$$), PetC (Rieske ISP), and PetD (subunit IV) . These subunits bind or coordinate five tightly bound metallo-redox prosthetic groups, including hemes f, $$b_p$$, $$b_n$$, $$c_n$$, and the 2Fe-2S Rieske iron-sulfur protein (ISP) .
The recombinant full-length Coffea arabica Cytochrome b6-f complex subunit 4 (petD) protein is expressed in E. coli with an N-terminal His tag . Key specifications of the recombinant protein are detailed below.
Component of the cytochrome b6-f complex. This complex facilitates electron transfer between Photosystem II (PSII) and Photosystem I (PSI), cyclic electron flow around PSI, and state transitions.