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Copper protein
Rusticyanin (RCN) is a copper protein with a type I copper center that plays an integral role in electron transfer. It can be extracted from the periplasm
Rusticyanin
Iron:rusticyanin reductase (EC 1.16.9.1, Cyc2) is an enzyme with systematic name Fe(II):rusticyanin oxidoreductase. This enzyme catalyses the following
Iron:rusticyanin_reductase
Topics referred to by the same term
Cyc2 may refer to: Iron:rusticyanin reductase, an enzyme Terpentetriene synthase, an enzyme This disambiguation page lists articles associated with the
Cyc2
Organisms that thrive under highly acidic conditions
"Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: a highly oxidizing cupredoxin with extreme acid stability". J Mol Biol
Acidophile
Iron oxidizing enzyme, Fe(II) to Fe(III) conversion
mitochondrial HEPH - Hephaestin Cox JC, Boxer DH (1986). "The role of rusticyanin, a blue copper protein, in the electron transport chain of Thiobacillus
Ferroxidase
corrinoid adenosyltransferase EC 1.16.9.1: iron:rusticyanin reductase EC 1.16.98.1: Now EC 1.16.9.1 iron:rusticyanin reductase EC 1.16.99.1: [Co(II) methylated
List_of_EC_numbers_(EC_1)
Protein family
membrane-associated copper-binding protein; pseudoazurin from Pseudomonas; rusticyanin from Thiobacillus ferrooxidans; stellacyanin from Rhus vernicifera (Japanese
Plastocyanin family of copper-binding proteins
Plastocyanin_family_of_copper-binding_proteins
Biochemical pathways used by microbes to satisfy energy needs
therefore requires large amounts of iron to be oxidized by the enzyme rusticyanin to facilitate the formation of proton motive force. Like sulfur oxidation
Microbial_metabolism
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