From Proteopedia
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Description
Enzyme
Ferredoxin-NADP+ reductase (FRN), also called ferredoxin-NADP+ oxidoreductase, is a flavoprotein which can be mainly found in chloroplasts, mitochondria and even bacteria.
In plants, this protein is a cellular component that binds to the stromal surface of the thylakoid membrane and which is involved in the last step of the photosynthetic electron transport chain.
Indeed, ferredoxin-NADP+ reductase is an enzyme that catalyzes the electron transfer between the electron carrier protein ferredoxin (Fd) and NADP(H).
Activity
Structure
Ferredoxin-NADP+ reductase of spinach has two structural domains :
- The first domain, at the N-ter of the protein, is an antiparallel beta barrel that contains the binding site for the FAD cofactor [1].
- The second domain, at the C-ter of the protein, contains an alpha-helix-beta strand fold [1]. This terminal domain is where the NADP+ binds [2].
The interface between these two domains is actually the active site of the ferredoxin-NADP+ reductase.
References
- ↑ 1.0 1.1 Aliverti A, Pandini V, Pennati A, de Rosa M, Zanetti G. Structural and functional diversity of ferredoxin-NADP(+) reductases. Arch Biochem Biophys. 2008 Jun 15;474(2):283-91. Epub 2008 Feb 16. PMID:18307973 doi:10.1016/j.abb.2008.02.014
- ↑ Paladini DH, Musumeci MA, Carrillo N, Ceccarelli EA. Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductases. Biochemistry. 2009 Jun 23;48(24):5760-8. PMID:19435322 doi:10.1021/bi9004232