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Cytochrome b 5 is a major reductant in vivo of human indoleamine 2,3‐dioxygenase expressed in yeast
Author(s) -
Vottero Eduardo,
Mitchell David A.,
Page Michael J.,
MacGillivray Ross T.A.,
Sadowski Ivan J.,
Roberge Michel,
Mauk A. Grant
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.034
Subject(s) - indoleamine 2,3 dioxygenase , yeast , chemistry , in vivo , cytochrome , biochemistry , biology , tryptophan , enzyme , genetics , amino acid
The evolutionary relationship of indoleamine 2,3‐dioxygenase (IDO) to some gastropod myoglobins suggests that IDO may undergo autoxidation in vivo such that one or more currently unidentified electron donors are required to maintain IDO heme iron in the active, ferrous state. To evaluate this hypothesis we have used yeast knockout mutants in combination with a recently developed yeast growth assay for IDO activity in vivo to demonstrate a role for cytochrome b 5 and cytochrome b 5 reductase in maintaining IDO activity in vivo.