Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.5 extracted from

  • Miner, K.D.; Pfister, T.D.; Hosseinzadeh, P.; Karaduman, N.; Donald, L.J.; Loewen, P.C.; Lu, Y.; Ivancich, A.
    Identifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase implications for oxidation of substrates bound at a site remote from the heme (2014), Biochemistry, 53, 3781-3789 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information residues Tyr71 and Tyr236 contribute primarily to the EPR spectrum of the tyrosyl radical. The heme distal-side Trp51 is involved in the intramolecular electron transfer between Tyr71 and the heme and formation of Tyr71 and Tyr236 radicals is independent of the [Fe(IV)=O Trp191+] radical intermediate. Tyr71 radical is the reactive species with the guaiacol substrate. Surface-exposed residue Tyr236 is the other radical site Saccharomyces cerevisiae ?
-
?