1H85

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L)

Summary for 1H85

• Entry DOI: 10.2210/pdb1h85/pdb
• Related: 1B2R 1BJK 1E62 1E63 1E64 1QUE 1QUF
• Descriptor: FERREDOXIN--NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, flavoprotein, nadp, electron transport
• Biological source: NOSTOC SP.
• Total number of polymer chains: 1
• Total formula weight: 34098.35

Authors

Hermoso, J.A.,Mayoral, T.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (deposition date: 2001-01-24, release date: 2001-11-28, Last modification date: 2023-12-13)

Primary citation

Marti-Nez-Julvez, M.,Nogues, I.,Faro, M.,Hurley, J.K.,Brodie, T.B.,Mayoral, T.,Sanz-Aparicio, J.,Hermoso, J.A.,Stankovich, M.T.,Medina, M.,Tollin, G.,Gomez-Moreno, C.
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
J.Biol.Chem., 276:27498-, 2001

PubMed Abstract: 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 are observed upon conservative replacement. Introduction of Ser residues produces relatively sizable alterations of the FAD redox potential, which can explain the modified behavior of these mutants. The introduction of bulky aromatic side chains appears to produce rearrangements of the side chains at the FNR/Fd interaction surface. Thus, subtle changes in the hydrophobic patch influence the rates of ET to and from Fd by altering the binding constants and the FAD redox potentials, indicating that these residues are especially important in the binding and orientation of Fd for efficient ET. These results are consistent with the structure reported for the Anabaena FNR.Fd complex.

PubMed: 11342548
DOI: 10.1074/JBC.M102112200

Experimental method

X-RAY DIFFRACTION (2.3 Å)