Table I.

Summary of high-spin (HS) ferric heme iron detected by optical spectroscopy and NRase activity towards m-nitroacetophenone 6 for WT and mutant CYP101A1 enzymes. <5%, (n.d., not detected), indicates that a shoulder at 390 nm could not be distinguished in optical spectra in the presence of d-camphor 1. All six enzymes catalyze the hydroxylation of 1 to 2, although with differences in rate and efficiency (see ref. [6] for details).

CYP101A1	% high-spin w/ camphor 1 bound	NRase activity
WT	>95%	Y
I160L	~35%	N
I160L/L166A	~80%	Y
I160L/L166F	<5% (n.d.)	N
I160L/L166T	~75%	Y
I160L/L166V	~50%	Y