Effect of water-soluble zinc porphyrin on the catalytic activity of fumarase for L-malate dehydration to fumarate.
In: New Journal of Chemistry, Jg. 47 (2023-10-14), Heft 38, S. 17679-17684
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Zugriff:
Fumarase from porcine heart (FUM; EC 4.2.1.2) is an enzyme that dehydrates L-malate in an aqueous medium to catalyze fumarate production. In the visible-light driven NADH regeneration with the system of an electron donor, water-soluble zinc porphyrin as a photosensitizer and pentamethylcyclopentadienyl rhodium 2,20-bipyridine complex ([Cp*Rh(bpy)(H 2 O)] 2+ ) and malate dehydrogenase from Sulfobus tokodaii (oxaloacetate-decarboxylating; MDH; EC 1.1.1.38), fumarate can be produced from CO 2 and pyruvate by dehydrating L-malate produced as an intermediate with FUM. To improve fumarate production efficiency in this system, it is necessary to study the interaction between FUM and water-soluble zinc porphyrin. In this work, the effect of water-soluble zinc or metal-free porphyrin derivatives, tetra(4-sulfonatophenyl)porphyrin, tetra- (4-carboxyphenyl)porphyrin, tetrakis(4-methylpyridyl)porphyrin or tetrakis(4-N,N,N-trimethylaminophenyl)-porphyrin on the catalytic activity of FUM for L-malate dehydration to fumarate was studied. It was found that the addition of anionic water-soluble zinc porphyrins, zinc tetra(4-sulfonatophenyl)porphyrin (ZnTPPS 4- ) and zinc tetra(4-carboxyphenyl)porphyrin (ZnTCPP 4- ) inhibited the catalytic activity of FUM. In particular, fumarate production with FUM was strongly suppressed in the addition of ZnTPPS 4- (reduced to about 16% compared to control experiments). On the other hand, the addition of cationic water-soluble zinc or metal-free porphyrins had little effect on the catalytic activity of FUM for L-malate dehydration to fumarate. Furthermore, UV-vis absorption and circular dichroism spectroscopic results suggested that ZnTPPS 4- binds to the substrate-binding site of FUM and inhibits fumarate production. [ABSTRACT FROM AUTHOR]
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Titel: |
Effect of water-soluble zinc porphyrin on the catalytic activity of fumarase for L-malate dehydration to fumarate.
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Autor/in / Beteiligte Person: | Takeuchi, Mika ; Amao, Yutaka |
Zeitschrift: | New Journal of Chemistry, Jg. 47 (2023-10-14), Heft 38, S. 17679-17684 |
Veröffentlichung: | 2023 |
Medientyp: | academicJournal |
ISSN: | 1144-0546 (print) |
DOI: | 10.1039/d3nj02900j |
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