Table 1.
Specific substrate-reducing activities of substrate-free DPOR, apo nitrogenase variant, and holo nitrogenase
| Enzyme | Activities (nmol⋅min−1⋅mg−1) |
|||||
| Chlide formation from 0.02 mM Pchlide | NH3 formation from 40 mM N3− | NH3 formation from 40 mM N2H4 | NH3 formation from 100% N2 | C2H4 formation from 60% C2H2 | C2H4 formation from 100% CO | |
| Substrate-free DPOR | 1.1 ± 0.1 | 1.2 ± 0.1 | 1.07 ± 0.01 | 0 (0) | 0 (0) | 0 (0) |
| Apo nitrogenase variant | 0 (0) | 2.4 ± 0.3 | 0.4 ± 0.2 | 0 (0) | 3.3 ± 0.5 | 0 (0) |
| Holo nitrogenase | 0 (0) | 624 ± 16 | 263 ± 2 | 481 ± 19 | 2216 ± 145 | 0.013 ± 0.001 |
Specific substrate-reducing activities of substrate-free DPOR, apo nitrogenase variant, and holo nitrogenase are shown. Substrate-free DPOR consists of L2 and (NB)2, whereas apo nitrogenase variant consists of NifH2 and apo (NifDK)2 variant. Data are presented as mean ± SD (n = 4). The lower detection limits were 0.08, 0.0005, and 0.001 nmol⋅min−1⋅mg−1 of protein for Chlide-, C2H4-, and NH3-formation, respectively.