Ferredoxin reductase may refer to:
Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.
A hydrogenosome is a membrane-enclosed organelle of some anaerobic ciliates, trichomonads, fungi, and animals. The hydrogenosomes of trichomonads produce molecular hydrogen, acetate, carbon dioxide and ATP by the combined actions of pyruvate:ferredoxin oxido-reductase, hydrogenase, acetate:succinate CoA transferase and succinate thiokinase. Superoxide dismutase, malate dehydrogenase (decarboxylating), ferredoxin, adenylate kinase and NADH:ferredoxin oxido-reductase are also localized in the hydrogenosome. It is nearly universally accepted that hydrogenosomes evolved from mitochondria.
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.
Sulfite reductase (ferredoxin) (EC 1.8.7.1, ferredoxin-sulfite reductase) is an enzyme with systematic name hydrogen-sulfide:ferredoxin oxidoreductase. This enzyme catalises the following chemical reaction
In enzymology, a 6-hydroxynicotinate reductase is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) (EC 1.2.7.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction
In enzymology, a ferredoxin–NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction:
In enzymology, a ferredoxin—nitrate reductase (EC 1.7.7.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a ferredoxin—nitrite reductase (EC 1.7.7.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylenetetrahydrofolate reductase (ferredoxin) (EC 1.5.7.1) is an enzyme that catalyzes the chemical reaction
Adrenodoxin reductase, was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.
Flavoprotein pyridine nucleotide cytochrome reductases catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases, plant and fungal NAD(P)H:nitrate reductases, cytochrome b5 reductases, cytochrome P450 reductases, sulphite reductases, nitric oxide synthases, phthalate dioxygenase reductase, and various other flavoproteins.
Oxidoreductase NAD-binding domain is an evolutionary conserved protein domain.
FNR may refer to:
Ferredoxin-thioredoxin reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important role in the ferredoxin/thioredoxin regulatory chain. It catalyzes the following reaction:
Ferredoxin:protochlorophyllide reductase (ATP-dependent) (EC 1.3.7.7), light-independent protochlorophyllide reductase) is an enzyme with systematic name ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase. This enzyme catalyses the following chemical reaction
7-Hydroxymethyl chlorophyll a reductase (EC 1.17.7.2, HCAR) is an enzyme with systematic name 71-hydroxychlorophyll a:ferredoxin oxidoreductase. This enzyme catalyses the following chemical reaction
Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.
Cytochrome P450 aromatic O-demethylase is a bacterial enzyme that catalyzes the demethylation of lignin and various lignols. The net reaction follows the following stoichiometry, illustrated with a generic methoxy arene: