Alkaline denaturation of the light-harvesting complex II from the purple bacterium Ectothiorhodospira sp.: kinetic evidence of the existence of the 780 nm upper exciton component of the B850 bacteriochlorophylls.
The light-harvesting complex II of the purple bacteria has two strong near-infrared electronic absorption bands around 800 (B800) and 850 (B850) nm, arising from the Q(y)() transitions of the bacteriochlorophyll a. In the present work, high concentrations of NaOH were used to study the destabilization of the complex of the Ectothiorhodospira sp. The majority of the bacteriochlorophylls were monomerized within 90 min of treatment. However, the kinetic patterns of the two near-infrared bands were remarkably different. After an instantaneous blue shift from 853 to 828 nm, B850 showed a first-order monomerization with a rate constant of -0.016 min(-1). This instantaneous blue shift was previously attributed to the deprotonation of a lysine and was independent of the monomerization process. The observed native B800 is in fact composed of two bands, one at 796 nm and the other at 780 nm. The band absorbing at 780 nm red shifted also instantaneously to 786-788 nm and then disappeared in a first-order process as B850. The other band absorbing at 796 nm has a two-step process of monomerization; after a rapid conversion a slower first-order process occurred with a rate constant of -0.025 min(-1). The similarity between the kinetic behaviors of B850 and the 780 nm band indicated a strong relationship between these two bands. Our interpretation of the results considers the 780 nm band as the upper exciton component of the B850 bacteriochlorophylls.
Buche
A
A
Estación Experimental de Aula Dei (CSIC), Apdo. 202, 50080 Zaragoza, Spain. abuche@eead.csic.es
Picorel
R
R
D001429:Bacteriochlorophylls / Q000737:chemistry / Q000378:metabolism*; D002021:Buffers; D004305:Dose-Response Relationship, Drug; D020587:Ectothiorhodospira / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D012972:Sodium Hydroxide / Q000494:pharmacology*; D013055:Spectrophotometry, Infrared
D001429:Bacteriochlorophylls; D002021:Buffers; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D012972:Sodium Hydroxide