Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: mapping the interaction sites of ferredoxin.

The Journal of biological chemistry - 14 Apr 2006

Saitoh Takashi, Ikegami Takahisa, Nakayama Masato, Teshima Keizo, Akutsu Hideo, Hase Toshiharu

Abstract excerpt

Plant ferredoxin serves as the physiological electron donor for sulfite reductase, which catalyzes the reduction of sulfite to sulfide. Ferredoxin and sulfite reductase form an electrostatically stabilized 1:1 complex for the intermolecular electron transfer. The protein-protein interaction between these proteins from maize leaves was analyzed by nuclear magnetic resonance spectroscopy. Chemical shift...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid
Share to Chromatography, Affinity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Electron Transport

Share to Ferredoxins

Share to Oxidoreductases Acting on Sulfur Group Donors

Share to Static Electricity

Source

Identifiers

PMID: 16469743
DOI: 10.1074/jbc.M510530200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: mapping the interaction sites of ferredoxin.PMID 16469743Read ↗

Biochemical and Biophysical Methods to Examine the Effects of Site-Directed Mutagenesis on Enzymatic Activities and Interprotein Interactions.Semantic proximity Read ↗

Molecular mechanism of negative cooperativity of ferredoxin-NADP+ reductase by ferredoxin and NADP(H): involvement of a salt bridge between Asp60 of ferredoxin and Lys33 of FNR.Semantic proximity Read ↗

Higher order structure contributes to specific differences in redox potential and electron transfer efficiency of root and leaf ferredoxins.Semantic proximity Read ↗

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.Semantic proximity Read ↗

An engineered pathway for the formation of protein disulfide bonds.Semantic proximity Read ↗

Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin.Semantic proximity Read ↗

Genetic, Biochemical, and Biophysical Methods for Studying FeS Proteins and Their Assembly.Semantic proximity Read ↗

Flavoprotein disulfide reductases: advances in chemistry and function.Semantic proximity Read ↗

Allostery in the ferredoxin protein motif does not involve a conformational switch.Semantic proximity Read ↗

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways.Semantic proximity Read ↗

Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.Semantic proximity Read ↗

Flavodoxin-mediated electron transfer from photosystem I to ferredoxin-NADP+ reductase in Anabaena: role of flavodoxin hydrophobic residues in protein-protein interactions.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.