Premium
Docking analysis of transient complexes: Interaction of ferredoxin‐NADP + reductase with ferredoxin and flavodoxin
Author(s) -
Medina Milagros,
Abagyan Ruben,
GómezMoreno Carlos,
FernandezRecio Juan
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21979
Subject(s) - flavodoxin , ferredoxin , ferredoxin—nadp(+) reductase , docking (animal) , electron transfer , reductase , crystallography , chemistry , biophysics , biochemistry , biology , enzyme , photochemistry , medicine , nursing
Ferredoxin (Fd) interacts with ferredoxin‐NADP + reductase (FNR) to transfer two electrons to the latter, one by one, which will finally be used to reduce NADP + to NADPH. The formation of a transient complex between Fd and FNR is required for the electron transfer (ET), and extensive mutational and crystallographic studies have been reported to characterize such protein–protein interaction. However, some aspects of the association mechanism still remain unclear. Moreover, in spite of their structural differences, flavodoxin (Fld) can replace Fd in its function and interact with FNR to transfer electrons with only slightly lower efficiency. Although crystallographic structures for the FNR:Fd association have been reported, experimental structural data for the FNR:Fld interaction are highly elusive. We have modeled here the interactions between FNR and both of its protein partners, Fd and Fld, using surface energy analysis, computational rigid‐body docking simulations, and interface side‐chain refinement. The results, consistent with previous experimental data, suggest the existence of alternative binding modes in these ET proteins. Proteins 2008. © 2008 Wiley‐Liss, Inc.