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. 1999 Aug 31;96(18):10056–10061. doi: 10.1073/pnas.96.18.10056

Table 2.

Biochemical properties of recombinant wild-type and mutant LHCII and CP29

Recombinant protein Binding site affected Reconstitution efficiency, % Chl a+b/ polypeptide Xanthophylls Chl/carotenoid ratio Chl-a/b ratio Chl-a polypeptide, no. Chl-b polypeptide, no. Stability at 60°C t1/2, min
CP29
 Wild type 100 8 2 4.00 3.00 6 2 4.2
 H245L B3 94 7 2 3.50 4.35 5.7 1.3 2.0
 H216F A2 75 7 2 3.10 2.53 5 2 4.0
 H114F A5 53 7 2 3.47 2.42 5 2 0.5
 Q230L A3 90 7 2 3.45 3.11 5.3 1.7 1.7
 R218L A4 0
 E111V A4 0
 E111V/R218L A4 45 7 2 3.85 2.50 5 2 3.3
 E166V B6 45 6 1 6.12 5.02 5 1 0.4
 E166Q B6 90 8 2 4.00 2.34 5.6 2.4 5.2
 R177L B5 0
 E174V B5 55 7 1.5 4.75 3.91 5.6 1.4 0.5
 R177L/E174V B5 0
 E213V A1 0
 R116L A1 0
 R116L/E213V A1 0
LHCII
 Wild type 100 12 3 4.02 1.4 7 5 ND
 Q131E B6 94 12 3 4.05 1.65 7.4 4.6 ND

Standard deviations: Chl-a/b ratio, 0.04 (8–12 independent measurements; Chl/xanthophyll ratio, 0.2 (six independent measurements). Reconstitution efficiency represents the yield in CP with respect to wild type. In the case of LHCII, 25% of the wild-type apoprotein used in reconstitution was recovered as CP. ND, not determined.