Correction: Fatty acid epoxidation by Collariella virescens peroxygenase and heme-channel variants

Abstract

The authors regret that, due to a re-estimation of the molar extinction coefficient of the enzyme here described, the values of several calculations presented in the paper must be amended. Such amendments concern the enzyme concentrations used in different parts of the manuscript that, due to the erroneous coefficient value initially used, were actually several times higher, and kcat values were therefore overestimated (for clarity the correct extinction coefficient is provided in the list of amendments below). The required amendments are the following:Page 719: • Right col., 4th line: 0.25 μM should be 1.4 μM • Right col., 13th line: 0.25–0.4 μM should be 1.4–2.3 μM • Right col., 31st line: 75 nM should be to 4.3 μM Page 720: • Fig. 2 caption, 4th line: 0.25–0.4 μM should be 1.4–2.3 μM Page 721: • Left col., 3rd line: 1 μM should be 6 μM • Right col., 26th line: “despite the higher turnover number of the C. virescens enzyme” should be replaced by “for the latter enzyme” • Fig. 4 caption, 4th line: 75 nM should be 4.3 μM Page 722: • Table 1: values of kcat and kcat/Km for CviUPO and F88L should read as: CviUPO kcat: 2.2 ± 0.05 (instead of 12.6 ± 0.3); CviUPO kcat/Km: 37.4 ± 3.9 (instead of 214 ± 23) F88L kcat: 1.2 ± 0.03 (instead of 7.0 ± 0.2); F88L kcat/Km: 39.2 ± 4.8 (instead of 224 ± 27) • Footnote of Table 2: 0.25–0.4 μM should be 1.4–2.3 μM Apart from the abovementioned amendments, the authors would like to add the following sentence, which was not present in the published article, providing the correct extinction coefficient of the enzyme: • Page 718, right col., 47th line (after the last sentence of UPO purification sub-section): The molar extinction coefficient of the enzyme was estimated (ε420 nm 114 mM−1 cm−1). Finally, it is important to mention that the above changes do not affect the conclusions of the paper that (as stated in the last sentence of the Abstract) basically concern: i) the possibility to enlarge the repertoire of UPOs available by E. coli expression of putative upo genes from genomes, etc. (a qualitative observation remaining valid after the changes); and ii) the effect of heme-channel mutations on the oxygenation pattern of unsaturated fatty acids by the enzyme (with the activity ratios between mutated and wild-type enzymes remaining unchanged after the correction, as shown in Table 2, etc.). The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers. © 2020 The Royal Society of Chemistry.