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. Author manuscript; available in PMC: 2015 Oct 21.
Published in final edited form as: FEBS J. 2014 Sep 19;281(20):4691–4704. doi: 10.1111/febs.12975

Table 1.

The reductive half-reaction of NQO1 P187S is compromised, thereby affecting its ability to accept electrons from NAD(P)H. Bimolecular rate constants (m−1·s−1) were determined for NQO1 proteins with NADH or NADPH as reducing agent. The absorption change of protein-bound FAD at 445 nm was monitored in a stopped-flow instrument at 4 °C.

Protein NADH kred (m−1·s−1) NADPH kred (m−1·s−1)
NQO1 (3.5 × 106) ± (1.0 × 106) (5.7 × 106) ± (2.7 × 106)
NQO1 P187S (1.2 × 104) ± (1.7 × 103) (8.5 × 104) ± (1.8 × 106)
NQO1 Δ50 (4.7 × 103) ± (0.7 × 103) (1.3 × 104) ± (0.1 × 104)
NQO1 P187S Δ50 (3.2 × 103) ± (0.2 × 103) (8.2 × 104) ± (0.2 × 104)