1h85
|
FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L)
OverviewOverview
In the ferredoxin-NADP(+) reductase (FNR)/ferredoxin (Fd) system, an, aromatic amino acid residue on the surface of Anabaena Fd, Phe-65, has, been shown to be essential for the electron transfer (ET) reaction. We, have investigated further the role of hydrophobic interactions in complex, stabilization and ET between these proteins by replacing three hydrophobic, residues, Leu-76, Leu-78, and Val-136, situated on the FNR surface in the, vicinity of its FAD cofactor. Whereas neither the ability of FNR to accept, electrons from NADPH nor its structure appears to be affected by the, introduced mutations, different behaviors with Fd are observed. Thus, the, ET interaction with Fd is almost completely lost upon introduction of, negatively charged side chains. In contrast, only subtle changes ... [(full description)]
About this StructureAbout this Structure
1H85 is a [Single protein] structure of sequence from [Anabaena sp.] with SO4 and FAD as [ligands]. Active as [[1]], with EC number [1.18.1.2]. Full crystallographic information is available from [OCA].
ReferenceReference
Role of a cluster of hydrophobic residues near the FAD cofactor in Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal complex formation and electron transfer to ferredoxin., Martinez-Julvez M, Nogues I, Faro M, Hurley JK, Brodie TB, Mayoral T, Sanz-Aparicio J, Hermoso JA, Stankovich MT, Medina M, Tollin G, Gomez-Moreno C, J Biol Chem. 2001 Jul 20;276(29):27498-510. Epub 2001 May 7. PMID:11342548
Page seeded by OCA on Mon Oct 29 19:10:36 2007