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. Author manuscript; available in PMC: 2017 Jan 1.
Published in final edited form as: Chem Sci. 2015 Sep 28;7:234–239. doi: 10.1039/c5sc02857d

Table 1.

Catalytic activity of wild-type myoglobin (Mb) and its variants in the oxidation of benzyl azide to benzaldehyde.[a]

graphic file with name nihms-729709-t0001.jpg
Entry Catalyst [catalyst]
/ mM		 pH Conv.[b] TON[c]
1 Hemin 0.02 8.0 19% 95
2 Hemin + imidazole
(1 mM)		 0.02 8.0 22% 110
3 WT Mb 0.001 8.0 18% 1,650
4 Mb(L29A) 0.001 8.0 19% 1,630
5 Mb(F43W) 0.001 8.0 23% 2,190
6 Mb(F43V) 0.001 8.0 32% 2,980
7 Mb(H64V) 0.001 8.0 41% 3,500
8 Mb(V68A) 0.001 8.0 15% 1,420
9 Mb(V68F) 0.001 8.0 6% 580
10 Mb(L29A,H64V) 0.001 8.0 36% 3,110
11 Mb(F43V,V68A) 0.001 8.0 42% 3,380
13 Mb(H64V,V68A) 0.001 8.0 49% 3,740
14 Mb(H64V,V68A) 0.001 7.0 77% 6,340
[a]

Reactions (400 μL) were conducted under anaerobic conditions with 10 mM BnN3 and 10 mM Na2S2O4 for 24 hours at room temperature.

[b]

Product yield based on conversion of initial 1a to 2a as determined by gas chromatography.

[c]

= nmol aldehyde / nmol catalyst. Errors in reported values are within ± 10%.