Unusual Peroxide-Dependent, Heme-Transforming Reaction Catalyzed by HemQ

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• 作者：Arianna I. Celis ; Bennett R. Streit ; Garrett C. Moraski ; Ravi Kant ; Timothy D. Lash ; Gudrun S. Lukat-Rodgers ; Kenton R. Rodgers ; Jennifer L. DuBois
• 刊名：Biochemistry
• 出版年：2015
• 出版时间：July 7, 2015
• 年：2015
• 卷：54
• 期：26
• 页码：4022-4032
• 全文大小：624K
• ISSN：1520-4995

文摘

A recently proposed pathway for heme b biosynthesis, common to diverse bacteria, has the conversion of two of the four propionates on coproheme III to vinyl groups as its final step. This reaction is catalyzed in a cofactor-independent, H₂O₂-dependent manner by the enzyme HemQ. Using the HemQ from Staphylococcus aureus (SaHemQ), the initial decarboxylation step was observed to rapidly and obligately yield the three-propionate harderoheme isomer III as the intermediate, while the slower second decarboxylation appeared to control the overall rate. Both synthetic harderoheme isomers III and IV reacted when bound to HemQ, the former more slowly than the latter. While H₂O₂ is the assumed biological oxidant, either H₂O₂ or peracetic acid yielded the same intermediates and products, though amounts significantly greater than the expected 2 equiv were required in both cases and peracetic acid reacted faster. The ability of peracetic acid to substitute for H₂O₂ suggests that, despite the lack of catalytic residues conventionally present in heme peroxidase active sites, reaction pathways involving high-valent iron intermediates cannot be ruled out.