In vitro demethoxycarbonylation of various chlorophyll analogs by a BciC enzyme View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-03

AUTHORS

Misato Teramura, Jiro Harada, Hitoshi Tamiaki

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. More... »

PAGES

163-171

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11120-018-0573-1

DOI

http://dx.doi.org/10.1007/s11120-018-0573-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1106610857

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30182280


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