title: Direct computer simulation of ferredoxin and FNR complex formation in solution.
abstract: Ferredoxin reduced by Photosystem I in light serves as an electron donor for the reduction of NADP(+) to NADPH, and this reaction is catalyzed by enzyme ferredoxin:NADP(+)-reductase (FNR). Kinetics and mechanisms of this reaction have been extensively studied experimentally by site-specific mutagenesis, laser flash photolysis and stopped-flow methods. We have applied a method of multiparticle computer simulation to study the effects of electrostatic interactions upon the reaction rate of Fd-FNR complex formation. Using the model we calculated rate constants of Fd-FNR complex formation for the wild-type proteins and some mutant forms of FNR at different values of ionic strength. Simulation revealed that electrostatic interactions play an important role in Fd-FNR complex formation and define its specificity.
authors.affiliation: Biological Faculty, Lomonosov Moscow State University, Moscow, Russia. kovalenko78@mail.ru
authors.forename: I B
authors.initials: IB
authors.lastname: Kovalenko
authors.forename: A N
authors.initials: AN
authors.lastname: Diakonova
authors.forename: A M
authors.initials: AM
authors.lastname: Abaturova
authors.forename: G Yu
authors.initials: GY
authors.lastname: Riznichenko
authors.forename: A B
authors.initials: AB
authors.lastname: Rubin
mesh_terms: D017033:Anabaena / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003198:Computer Simulation; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005288:Ferredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D055672:Static Electricity
chemical_list: D001426:Bacterial Proteins; D005288:Ferredoxins; D005287:Ferredoxin-NADP Reductase