The auxiliary [4Fe-4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer

Chemical Science
Melanie KühnerGunhild Layer

Abstract

The heme synthase AhbD catalyzes the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme during the alternative heme biosynthesis pathway occurring in sulfate-reducing bacteria and archaea. AhbD belongs to the family of Radical SAM enzymes and contains two [4Fe-4S] clusters. Whereas one of these clusters is required for substrate radical formation, the role of the second iron-sulfur cluster is not known. In this study, the function of the auxiliary cluster during AhbD catalysis was investigated. Two single cluster variants of AhbD from M. barkeri carrying either one of the two clusters were created. Using these enzyme variants it was shown that the auxiliary cluster is not required for substrate binding and formation of the substrate radical. Instead, the auxiliary cluster is involved in a late step of AhbD catalysis most likely in electron transfer from the reaction intermediate to a final electron acceptor. Moreover, by using alternative substrates such as coproporphyrin III, Cu-coproporphyrin III and Zn-coproporphyrin III for the AhbD activity assay it was observed that the central iron ion of the porphyrin substrate also participates in the electron tr...Continue Reading

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Citations

Dec 29, 2017·The Journal of Biological Chemistry·Vera HaskampDieter Jahn
Sep 26, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Gunhild Layer
Oct 27, 2018·Biochemistry·Bin Li, Jennifer Bridwell-Rabb
Sep 8, 2021·Journal of the American Chemical Society·Ronald A BesandreHung-Wen Liu

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Methods Mentioned

BETA
cleavage assay
PCR
electrophoresis
fluorescence

Software Mentioned

Easyspin Matlab
esfit
Matlab
Easyspin
OriginPro

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