In vitro demethoxycarbonylation of various chlorophyll analogs by a BciC enzyme.

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 Res

journal_title

Photosynthesis research

authors

Teramura M,Harada J,Tamiaki H

doi

10.1007/s11120-018-0573-1

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

163-171

issue

1-3

eissn

0166-8595

issn

1573-5079

pii

10.1007/s11120-018-0573-1

journal_volume

139

pub_type

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