Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13

- Genes encoding 'Type II FMOs' CFMO and PSFMO were selected for diversity in the NADPH binding loop.
- CFMO and PSFMO were shown to both accept either NADH or NADPH as cofactor in the reduction of FAD.
- The activities with both NADPH and NADH have been evaluated in the oxidation of sulfide substrates.
- Structures of CFMO and PSFMO were solved, revealing the nature of the NADPH phosphate binding loop.