Abstract:
:We present the detailed characterization on the reconstitution of two cyclic tetrapyrrole pigments that have the same substituents but differ in the degree of hydrogenation in the macrocycles from bacteriochlorophyll (BChl) a (7,8,17,18-tetrahydroporphyrin) into the binding sites of B800 BChl a in light-harvesting complex 2 (LH2) of purple photosynthetic bacteria. Both 3-acetyl chlorophyll (Chl) a (17,18-dihydroporphyrin) and 3-acetyl protochlorophyll (PChl) a (porphyrin) were inserted into the B800-binding pockets in LH2, indicating that these pockets allow alteration of the degree of hydrogenation in the cyclic tetrapyrroles. Redshifts of the Qy peak positions of 3-acetyl (P)Chl a by insertion into the B800-binding sites were smaller than that of BChl a. The relative Qy absorbance of 3-acetyl (P)Chl a to B850 BChl a in the reconstituted proteins was significantly smaller than that of B800 BChl a in native LH2 in spite of their high occupancy in the B800-binding sites. These are ascribable to the smaller dipole strengths of 3-acetyl (P)Chl a. We also performed the coreconstitution of both 3-acetyl Chl a and BChl a into the nine B800-binding sites in LH2, indicating that the affinity of 3-acetyl Chl a to the B800-cavity was slightly higher than that of BChl a.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Saga Y,Miyagi Kdoi
10.1111/php.12919subject
Has Abstractpub_date
2018-07-01 00:00:00pages
698-704issue
4eissn
0031-8655issn
1751-1097journal_volume
94pub_type
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