▁re duct ase : ad ren odox in : P 4 5 0 . ▁Both ▁spect ro scop ic ▁studies ▁of ▁ad ren odox in ▁binding ▁to ▁P 4 5 0 s cc ▁and ▁kin etic ▁studies ▁in ▁the ▁presence ▁of ▁varying ▁concentr ations ▁of ▁ad ren odox in ▁re duct ase ▁demonstrated ▁that ▁the ▁re duct ase ▁compet es ▁with ▁P 4 5 0 s cc ▁for ▁binding ▁to ▁ad ren odox in . ▁These ▁results ▁demonstrated ▁that ▁the ▁formation ▁of ▁a ▁functional ▁t ern ary ▁complex ▁is ▁not ▁possible . ▁From ▁these ▁studies , ▁it ▁was ▁concluded ▁that ▁the ▁binding ▁sites ▁of ▁ad ren odox in ▁to ▁its ▁re duct ase ▁and ▁to ▁P 4 5 0 ▁are ▁over la pping ▁and , ▁as ▁a ▁consequence , ▁ad ren odox in ▁functions ▁as ▁a ▁mobile ▁electron ▁sh utt le ▁between ▁re duct ase ▁and ▁P 4 5 0 . ▁These ▁conclus ions ▁have ▁been ▁confirmed ▁by ▁struct ural ▁analysis ▁of ▁ad ren odox in ▁and ▁P 4 5 0 ▁complex . ▁ ▁The ▁process ▁of ▁electron ▁transfer ▁from ▁N AD PH ▁to ▁P 4 5 0 s cc ▁is ▁not ▁tight ly ▁couple d ; ▁that ▁is , ▁during ▁electron ▁transfer ▁from ▁ad ren odox in ▁re duct ase ▁via ▁ad ren odox in ▁to ▁P 4 5 0 s cc , ▁a ▁certain ▁portion ▁of ▁the ▁electrons ▁leak ▁outside ▁of ▁the ▁chain ▁and ▁react ▁with ▁O 2 , ▁generating ▁super ox ide ▁radical s . ▁Ster oid ogen ic ▁cells