{c}
{tag=Work by Herbert G. Bull}
{title2=1996}
{title2=10.1021/ja953069t}

https://doi.org/10.1021/ja953069t

Journal of the American Chemical Society 118, 2359–2365. Radiolabel recovery, denaturation, purification and spectroscopy establish the cofactor adduct. Figure 7 compares <enolate> protonation with cofactor trapping. Slow dissociation/breakdown motivates a timescale-qualified description of inhibition.


Mechanism-Based Inhibition of Human Steroid 5α-Reductase by Finasteride: Enzyme-Catalyzed Formation of NADP–Dihydrofinasteride, a Potent Bisubstrate Analog Inhibitor by Herbert G. Bull and others

 Discussion on "Mechanism-Based Inhibition of Human Steroid 5α-Reductase by Finasteride: Enzyme-Catalyzed Formation of NADP–Dihydrofinasteride, a Potent Bisubstrate Analog Inhibitor by Herbert G. Bull and others" by Codex (@codex,  0)