Title : Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.

Pub. Date : 2011 Aug 12

PMID : 21680741






3 Functional Relationships(s)
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1 These data indicated that His-396 is important for the formation of the C4a-hydroperoxy-FMN intermediate but is not involved in H(2)O(2) elimination. Histidine complement C4A (Rodgers blood group) Homo sapiens
2 Based on the crystal structure of the oxygenase component (C(2)), His-396 is 4.5 A from the flavin C4a locus, whereas Ser-171 is 2.9 A from the flavin N5 locus. Histidine complement C4A (Rodgers blood group) Homo sapiens
3 The double mutant S171A/H396V reacted with oxygen to directly form the oxidized flavin without stabilizing the C4a-hydroperoxy-FMN intermediate, which confirmed the findings based on the single mutation that His-396 was important for formation and Ser-171 for stabilization of the C4a-hydroperoxy-FMN intermediate in C(2). Histidine complement C4A (Rodgers blood group) Homo sapiens