Biflaviolin synthase (EC 1.14.19.69, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase.[1][2] This enzyme catalyses two related chemical reactions:

2
 
2D representation of the chemical structure of Q27093505.
flaviolin
+ 2 reduced
ferredoxin + 2 H+
 
 
O2
2 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27122811.
3,3'-biflaviolin
+ 2 oxidised
ferredoxin
 

The reaction is an oxidative coupling of phenols which forms a dimer of the starting material. The alternative isomer, 3,8'-biflaviolin, is also producted. Biflaviolin synthase is a cytochrome P450 enzyme, isolated from the soil-dwelling bacterium Streptomyces coelicolor.[3]

References

  1. ↑ Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR (March 2005). "Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2". The Journal of Biological Chemistry. 280 (12): 11599–607. doi:10.1074/jbc.M410933200. PMID 15659395.
  2. ↑ Zhao B, Guengerich FP, Voehler M, Waterman MR (December 2005). "Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer". The Journal of Biological Chemistry. 280 (51): 42188–97. doi:10.1074/jbc.M509220200. PMID 16239228.
  3. ↑ Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR (July 2007). "Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2". Biochemistry. 46 (30): 8725–33. doi:10.1021/bi7006959. PMID 17614370.
source: https://en.wikipedia.org/wiki/Biflaviolin_synthase