Table I.
Enzyme | Rubisco Activation
|
ATPase Activity
|
Rubisco Activation: ATPase
|
|||
---|---|---|---|---|---|---|
Activitya | RWT | Activityb | RWT | Ratio | RWT | |
% | % | % | ||||
43-kD RWT | 4.2 | – | 0.55 | – | 7.8 | – |
Q111D | 8.2 | 190 | 0.78 | 140 | 10.6 | 140 |
Q111E | 10.0 | 240 | 0.68 | 120 | 14.7 | 190 |
Q111S | 2.3 | 55 | 0.35 | 64 | 6.5 | 83 |
Rubisco activation was determined by following phosphoglyceric acid production in a coupled spectrophotometric assay. ATPase activity in the absence of ADP was measured by a spectrophotometric assay modified from Robinson and Portis (1989). Rates represent steady-state values averaged over a 2-min time span. The Rubisco activation to ATPase ratio is a measure of the coupling efficiency. The results are the average of duplicate assays.
Units of activity are μmol CO2 min−1 mg−1 Rubisco min−1 mg−1 protein.
Units of activity are μmol ADP min−1 mg protein−1.