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Table S1. Maximum ω-OHFA yields, product distributions and other by-products obtained with resting E. coli cells harbouring wild-type CYP153AM. aq. or variant CYP153AM. aq. G307A fused to the reductase domain of P450 BM3.

Table S2. Maximum ω-OHFA yields and product distributions obtained with resting E. coli cells harbouring variant CYP153AM. aq. G307A fused to the reductase domain of P450 BM3 in a small-scale fermenter using C12-FA.

Table S3. Maximum ω-OHFA yields, product distributions and other by-products obtained with resting E. coli cells harbouring variant CYP153AM. aq. G307A fused to the reductase domain of P450 BM3 in a small-scale fermenter using C12-FAME.

Table S4. Oligonucleotide primers used for the construction of CYP153AM. aq. self-sufficient fusions, natural redox partners and alkL via PCR.

Fig. S1. Acetate and hydrogen peroxide (H2O2) concentrations in whole-cell biotransformations of dodecanoic acid by resting E. coli JM109 cells harbouring the pJOE-CPR2mut vector construct.

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