While direct structural data for Cyanothece sp. PsbH is limited, homology modeling suggests a conserved α-helical domain (Thr36–Ser60) critical for membrane integration .
PsbH stabilizes the PSII reaction center by:
Enhancing D1 Protein Assembly: PsbH interacts with the D1 protein (encoded by psbA), facilitating PSII repair under photoinhibitory conditions .
Modulating Electron Transport: In Cyanothece 51142, PSII activity peaks during nitrogenase-mediated H₂ production, correlating with increased psbA/psbD expression . Though PsbH dynamics are not explicitly detailed, its structural homology to Synechocystis PsbH implies analogous roles in maintaining PSII efficiency .
Recombinant PsbH is used to study:
PSII Assembly Mechanisms: PsbH-deficient mutants show impaired PSII recovery after photodamage .
Stress Responses: In Synechocystis, PsbH expression increases under high-light stress, suggesting its role in photoprotection .
Expression Challenges: Cyanothece sp. PsbH may require codon optimization for E. coli due to genetic divergence .
Post-Translational Modifications: Native PsbH in cyanobacteria is phosphorylated, but recombinant versions lack these modifications unless engineered .
Current gaps include:
KEGG: cyp:PCC8801_1645
STRING: 41431.PCC8801_1645