Место издания:Komarov Botanical Institute of the Russian Academy of Sciences St. Petersburg
Первая страница:183
Последняя страница:183
Аннотация:We investigated molecular mechanisms of interactions between ferredoxin, ferredoxin:NADP+-reductase (FNR) and hydrogenase using the method of multiparticle Brownian modeling developed by our group.
In this method, protein molecules are presented as rigid structures with fixed charges created by cofactors and amino acid residues. Molecules can be placed in a media imitating solution or in a structured environment imitating a chloroplast. Proteins move due to Brownian force and electrostatic forces orienting in each other’s electric field and forming complexes necessary for electron transfer [1].
We have studied competition between FNR and hydrogenase for ferredoxin. It is known that during illumination chloroplast stroma becomes more alkaline, so we investigated how pH affects the rate of interactions between ferredoxin and FNR and ferredoxin and hydrogenase. At pH from 5.0 to 9.0 the rate constant of complex formation between ferredoxin and FNR does not change significantly.
However, the rate of interaction between ferredoxin and hydrogenase dramatically depends on pH: at the pH range from 6.0 to 8.0 it increases three-fold. This result indicates different mechanisms of regulation of ferredoxin interaction with its protein partners.
One of the potential approaches to increasing hydrogen production is genetic engineering. Introduction of point mutations can potentially increase ferredoxin affinity to hydrogenase and decrease its affinity to FNR. We simulated several point mutations on ferredoxin and identified the most promising for increasing hydrogen yield.
The study was performed with financial support from the Russian Foundation for Basic Research, grant No. 17-04-00676А.