[HTML][HTML] Chloroplast-targeted ferredoxin-NADP+ oxidoreductase (FNR): Structure, function and location

P Mulo - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2011 - Elsevier
Ferredoxin-NADP+ oxidoreductase (FNR) is a ubiquitous flavin adenine dinucleotide (FAD)-
binding enzyme encoded by a small nuclear gene family in higher plants. The chloroplast …

Interaction and electron transfer between ferredoxin–NADP+ oxidoreductase and its partners: structural, functional, and physiological implications

P Mulo, M Medina - Photosynthesis research, 2017 - Springer
Abstract Ferredoxin–NADP+ reductase (FNR) catalyzes the last step of linear electron
transfer in photosynthetic light reactions. The FAD cofactor of FNR accepts two electrons …

Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+

M Medina - The FEBS journal, 2009 - Wiley Online Library
This minireview covers the research carried out in recent years into different aspects of the
function of the flavoproteins involved in cyanobacterial photosynthetic electron transfer from …

Theoretical Study of the Mechanism of the Hydride Transfer between Ferredoxin–NADP+ Reductase and NADP+: The Role of Tyr303

I Lans, M Medina, E Rosta, G Hummer… - Journal of the …, 2012 - ACS Publications
During photosynthesis, ferredoxin–NADP+ reductase (FNR) catalyzes the electron transfer
from ferredoxin to NADP+ via its FAD cofactor. The final hydride transfer event between FNR …

Crystal structure analysis of Bacillus subtilis ferredoxin‐NADP+ oxidoreductase and the structural basis for its substrate selectivity

H Komori, D Seo, T Sakurai, Y Higuchi - Protein Science, 2010 - Wiley Online Library
Bacillus subtilis yumC encodes a novel type of ferredoxin‐NADP+ oxidoreductase (FNR)
with a primary sequence and oligomeric conformation distinct from those of previously …

Retuning the potential of the electrochemical leaf

MM Dolińska, AJ Kirwan, CF Megarity - Faraday Discussions, 2024 - pubs.rsc.org
The electrochemical leaf enables the electrification and control of multi-enzyme cascades by
exploiting two discoveries:(i) the ability to electrify the photosynthetic enzyme ferredoxin …

Solvent dynamics play a decisive role in the complex formation of biologically relevant redox proteins

EM Adams, O Lampret, B König, T Happe… - Physical Chemistry …, 2020 - pubs.rsc.org
Electron transfer processes between proteins are vital in many biological systems. Yet, the
role of the solvent in influencing these redox reactions remains largely unknown. In this …

Mechanism of the Hydride Transfer between Anabaena Tyr303Ser FNRrd/FNRox and NADP+/H. A Combined Pre-Steady-State Kinetic/Ensemble-Averaged …

I Lans, JR Peregrina, M Medina… - The Journal of …, 2010 - ACS Publications
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH
during photosynthesis. The hydride-transfer reactions between the Anabaena mutant …

[HTML][HTML] Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes

A Sánchez-Azqueta, DL Catalano-Dupuy… - … et Biophysica Acta (BBA …, 2014 - Elsevier
Kinetic isotope effects in reactions involving hydride transfer and their temperature
dependence are powerful tools to explore dynamics of enzyme catalytic sites. In plant-type …

[HTML][HTML] Role of specific residues in coenzyme binding, charge–transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase

JR Peregrina, A Sánchez-Azqueta, B Herguedas… - … et Biophysica Acta (BBA …, 2010 - Elsevier
Two transient charge–transfer complexes (CTC) form prior and upon hydride transfer (HT) in
the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with …