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. 2011 May 13;16(6):899–912. doi: 10.1007/s00775-011-0789-4

Table 2.

Spectroscopic properties and yields of the CYP102A1 M11 mutants

No. Residue Reduced-CO difference spectra P450 yield (nmol/L growth medium)
Maximum (nm) A 450/A 420 ratio
Nonpolar side chain
 1 Phe87 450 >100 165
 2 Gly87 423, 449 78 148
 3 Ala87 449 >100 51
 4 Leu87 449 >100 237
 5 Ile87 449 >100 581
 6 Val87a 449 >100 666
 7 Met87 423, 448 12.1 344
 8 Pro87 420 ND NQ
 9 Trp87 450 >100 27
Uncharged polar side chain
 10 Ser87 422 ND NQ
 11 Thr87 449 >100 203
 12 Asn87 421, 450 1.2 132
 13 Gln87 448 >100 49
 14 Tyr87 448 >100 585
 15 Cys87 450 >100 41
Charged polar side chain
 16 Lys87 448 >100 91
 17 Arg87 449 >100 173
 18 His87 423, 450 5.8 80
 19 Asp87 420 ND NQ
 20 Glu87 420 ND NQ

ND no detectable peak at 450 nm, NQ not quantifiable owing to the absence of a peak at 450 nm

aCYP102A1 M11 containing R47L, E64G, F81I, F87V, E143G, L188Q, E267V, and G415S [9]