Significance: Several redox compounds, including respiratory burst oxidase homologs (Rboh) and iron chelate reductases have been identified in animal and plant plasma membrane (PM). Studies using molecular biological, biochemical, and proteomic approaches suggest that PM redox systems of plants are involved in signal transduction, nutrient uptake, transport, and cell wall-related processes. Function of PM-bound redox systems in oxidative stress will be discussed.
Recent advances: Present knowledge about the properties, structures, and functions of these systems are summarized. Judging from the currently available data, it is likely that electrons are transferred from cytosolic NAD(P)H to the apoplast via quinone reductases, vitamin K, and a cytochrome b561. In tandem with these electrons, protons might be transported to the apoplastic space.
Critical issues: Recent studies suggest localization of PM-bound redox systems in microdomains (so-called lipid or membrane rafts), but also organization of these compounds in putative and high molecular mass protein complexes. Although the plant flavocytochrome b family is well characterized with respect to its function, the molecular mechanism of an electron transfer reaction by these compounds has to be verified. Localization of Rboh in other compartments needs elucidation.
Future directions: Plant members of the flavodoxin and flavodoxin-like protein family and the cytochrome b561 protein family have been characterized on the biochemical level, postulated localization, and functions of these redox compounds need verification. Compositions of single microdomains and interaction partners of PM redox systems have to be elucidated. Finally, the hypothesis of an electron transfer chain in the PM needs further proof.