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. Author manuscript; available in PMC: 2009 Nov 4.
Published in final edited form as: Chem Res Toxicol. 2008 Nov;21(11):2073–2081. doi: 10.1021/tx800140y

Table I.

Comparison of observed cytochrome c oxidase (complex IV) turnover numbers during single and dual inhibition by CO, KCN, NO, CO + KCN, NO + KCN, NO + CO.

Inhibitor {concentration} Turnover number (kcat, s-1)#
Uninhibited control* 346 ± 28
CO {0.5 mM} 190 ± 21
KCN {50 nM} 136 ± 8
NO {0.5 μM} 184 ± 30
CO {0.5 mM} & KCN {50 nM} 109 ± 9
KCN {50 nM} & NO {0.5 μM} 176 ± 8
NO {0.5 μM} & CO {0.5 mM} 182 ± 11
*

1.2 nM enzyme, pH 7.4 in 0.1 M sodium phosphate buffer, 1 mM EDTA, 0.05% lauryl maltoside, 22 °C.

#

Calculated from fits in Figure 1A, quoted errors are standard deviations.