a ferredoxin fold is a common α+β protein fold with a signature βαββαβ secondary structure along its backbone. Structurally, the ferredoxin fold can...

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic...

enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction 2 reduced ferredoxin + NADP+ + H+...

β-strands are therefore mostly antiparallel. Common examples include the ferredoxin fold, ribonuclease A, and the SH2 domain. α/β proteins are a class of structural...

pattern of six secondary structure elements βαββαβ is the signature of a ferredoxin fold. Both protein and nucleic acid secondary structures can be used to...

Ferredoxin-thioredoxin reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important...

Flavohaemoglobins (FHb): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD/FAD-binding domain. FHb provides protection against...

7.7) uses ATP and ferredoxin: protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate...

(Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double...

NADH:cytochrome b5 reductase have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase: the FAD-binding domain (N-terminal) has...