Abstract:
:Unique light-harvesting antennas in the green sulfur bacterium Chlorobaculum tepidum, called chlorosomes, consist of self-aggregates of bacteriochlorophyll (BChl) c. In the biosynthesis of BChl c, BciC demethoxycarbonylase removes the C132-methoxycarbonyl group to facilitate the self-aggregation of BChl c. We previously reported the in vitro BciC-enzymatic reactions and discussed the function of this enzyme in the biosynthesis of BChl c. This study aims to examine the substrate specificity of BciC in detail using several semi-synthetic (bacterio)chlorophyll derivatives. The results indicate that the substrate specificity of BciC is measurably affected by structural changes on the A/B rings including the bacteriochlorin π-systems. Moreover, BciC showed its activity on a Zn-chelated chlorophyll derivative. On the contrary, BciC recognized structural modifications on the D/E rings, including porphyrin pigments, which resulted in the significant decrease in the enzymatic activity. The utilization of BciC provides mild conditions that may be useful for the in vitro preparation of various chemically (un)stable chlorophyllous pigments.
journal_name
Photosynth Resjournal_title
Photosynthesis researchauthors
Teramura M,Harada J,Tamiaki Hdoi
10.1007/s11120-018-0573-1subject
Has Abstractpub_date
2019-03-01 00:00:00pages
163-171issue
1-3eissn
0166-8595issn
1573-5079pii
10.1007/s11120-018-0573-1journal_volume
139pub_type
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journal_title:Photosynthesis research
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