The effects of QB-binding D1-protein mutations on the phenotypic characteristics and on hydrogen production of sulfur-deprived Chlamydomonas reinhardtii P. A. Dang. cultures were investigated. The mutation involved one (D240) or double (D23940) amino-acid deletions at positions 240 and 239240, respectively, in the loop connecting helices D and E of the D1 protein. Phenotypic characterization of the mutants showed the following peculiarities as compared to the wildtype (WT): (i) a higher sensitivity to photoinhibition, (ii) a reduced amount of chl per dry weight and per cell, (iii) a higher respiration-to-photosynthesis ratio, (iv) a higher carbohydrate accumulation during the aerobic phase, and (v) a higher synthesis of xanthophyll-cycle pigments. These differences were translated into a 12- to 18-fold higher hydrogen biogas production.
Phenotypic characterization and hydrogen production in Chlamydomonas reinhardtii QB binding D1 protein mutants under sulfur starvation: changes in chlorophyll fluorescence and pigment composition
Cecilia Faraloni;Giuseppe Torzillo
2010
Abstract
The effects of QB-binding D1-protein mutations on the phenotypic characteristics and on hydrogen production of sulfur-deprived Chlamydomonas reinhardtii P. A. Dang. cultures were investigated. The mutation involved one (D240) or double (D23940) amino-acid deletions at positions 240 and 239240, respectively, in the loop connecting helices D and E of the D1 protein. Phenotypic characterization of the mutants showed the following peculiarities as compared to the wildtype (WT): (i) a higher sensitivity to photoinhibition, (ii) a reduced amount of chl per dry weight and per cell, (iii) a higher respiration-to-photosynthesis ratio, (iv) a higher carbohydrate accumulation during the aerobic phase, and (v) a higher synthesis of xanthophyll-cycle pigments. These differences were translated into a 12- to 18-fold higher hydrogen biogas production.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.