Article
Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase.
Biochemistry - 3 Oct 1995
Calcaterra N B, Picó G A, Orellano E G, Ottado J, Carrillo N, Ceccarelli E A
Abstract excerpt
The contribution made by tyrosine 308 to the stability of pea ferredoxin-NADP+ reductase was investigated using site-directed mutagenesis. The phenol side chain of the invariant carboxyl terminal tyrosine is stacked coplanar to the isoalloxazine moiety of the FAD cofactor. Fluorescence measurements indicate that this interaction plays a significant role in FAD fluorescent quenching by the reductase apoprotein....
Topics
- Binding Sites
- Enzyme Stability
- Ferredoxin-NADP Reductase
- Flavin-Adenine Dinucleotide
- Hot Temperature
- Mutation
- Pisum sativum
- Protein Denaturation
- Spectrometry, Fluorescence
- Tyrosine