Table 2.
Sample | Methanotroph | Substrate | Reductant | Turnover number per protomer (s−1) | Specific activity (nmol mg total protein−1 min−1) | Refs |
---|---|---|---|---|---|---|
Cells producing pMMO | M. capsulatus (Bath) | propylene | formate | 1.4−2.5a | 167–300 | 136,162 |
M. trichosporium OB3b | methane | NA | 0.68–2.5b | 82–300 | 28,357 | |
Membrane-bound pMMO | M. capsulatus (Bath) | methane | NADH | 0.083–0.146c | 40–70 | 59,154 |
duroquinol | 0.025–0.042d | 12−20 | 59,154 | |||
propylene | NADH | 0.044–0.246e | 21–118 | 136,173 | ||
duroquinol | 0.033−0.179e | 16−86 | 136,173 | |||
M. sp. Rockwell | methane | NADH | 0.017–0.024d,f | 8–11.5 | 59,179 | |
duroquinol | 0.004–0.006d,f | 1.8–3 | 59,179 | |||
M. alcaliphilum 20Z | methane | NADH | 0.006c,f | 3 | 154 | |
duroquinol | 0 | 0 | 154 | |||
Purified pMMO in DDMg | M. capsulatus (Bath) | methane | NADH | 0 | 0 | 154 |
duroquinol | 0.002h,i | 1 | 60,154 | |||
M. capsulatus (Bath) | propylene | NADH | 0 | 0 | 136,173 | |
duroquinol | 0.032–0.21i,j | 18–126 | 136,173 | |||
M. sp. Rockwell | methane | NADH | 0 | 0 | 59 | |
duroquinol | 0 | 0 | 59 | |||
M. alcaliphilum 20Z | methane | NADH | 0 | 0 | 154 | |
duroquinol | 0 | 0 | 154 | |||
Purified pMMO in bicelles | M. capsulatus (Bath) | methane | NADH | 0.009f,g | 5.2 | 154 |
duroquinol | 0.006f,h | 3.5 | 154 | |||
M. alcaliphilum 20Z | methane | NADH | 0 | 0 | 154 | |
duroquinol | 0.007f,h | 4.4 | 154 | |||
Purified pMMO in nanodiscsi | ||||||
DMPCg | M. capsulatus (Bath) | methane | duroquinol | 0.005h | 3 | 60 |
POPCg | M. capsulatus (Bath) | 0.009h | 5.4 | 60 | ||
native lipids | M. capsulatus (Bath) | 0.012h | 7.2 | 60 | ||
POPCg | M. sp. Rockwell | methane | duroquinol | 0.011g | 6.6 | 179 |
POPCe | M. alcaliphilum 20Z | methane | duroquinol | 0 | 0 | 60 |
Calculated from rate of propylene epoxidation monitored by gas chromatography (GC) and assuming pMMO is 20% of the total protein.
Calculated from rate of methane uptake and assuming that pMMO is 20% of the total protein.
Calculated from rate of conversion of 13CH4 to 13CH3OH monitored by GC/mass spectrometry (GC/MS) and assuming that membrane-bound protein is 80% pMMO.
Calculated from rate of conversion of CH4 to CH3OH monitored by GC and assuming that membrane-bound protein is 80% pMMO. Values from ref 59 were converted to 13C values by applying a correction factor of 0.5.154
Calculated from rate of propylene epoxidation monitored by GC and assuming that membrane-bound protein is 80% pMMO.
Activity assay was performed at 30 °C. All other activity assays were performed at 45 °C.
Abbreviations used: DDM, n-dodecyl-β-D-maltoside; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; POPC, 1-palmitoyl-2-oleoylphosphatidylcholine.
Calculated from rate of conversion of 13CH4 to 13CH3OH monitored by GC/MS.
The samples used for the M. capsulatus (Bath) pMMO crystal structure determination were not assessed for methane oxidation activity and did not exhibit propylene epoxidation activity.151
Calculated from rate of propylene epoxidation monitored by GC.