Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis.

doi:10.1074/jbc.M313851200

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

Back to search

Article

Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis.

The Journal of biological chemistry - 16 Apr 2004

Glauser Dominique A, Bourquin Florence, Manieri Wanda, Schürmann Peter

Abstract excerpt

Ferredoxin:thioredoxin reductase (FTR) is a key regulatory enzyme of oxygenic photosynthetic cells involved in the reductive regulation of important target enzymes. It catalyzes the two-electron reduction of the disulfide of thioredoxins with electrons from ferredoxin involving a 4Fe-4S cluster and an adjacent active-site disulfide. We replaced Cys-57, Cys-87, and His-86 in the active site of Synechocystis FTR by...

Topics

Bacterial Proteins
Cyanobacteria
Iron-Sulfur Proteins
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Oxidoreductases
Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 14769790
DOI: 10.1074/jbc.M313851200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics