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Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu + ‐ ATPase mutant copA − of R ubrivivax gelatinosus
Author(s) -
Azzouzi Asma,
Steunou AnneSoisig,
Durand Anne,
KhalfaouiHassani Bahia,
Bourbon Marieline,
Astier Chantal,
Bollivar David W.,
Ouchane Soufian
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12188
Subject(s) - biochemistry , biology , mutant , oxidase test , atpase , tetrapyrrole , cytochrome c oxidase , enzyme , gene
Summary Two genes encoding structurally similar C opper P 1B ‐type ATPases can be identified in several genomes. Notwithstanding the high sequence and structural similarities these ATPases held, it has been suggested that they fulfil distinct physiological roles. In deed, we have shown that the Cu + ‐ ATPase CtpA is required only for the activity of cuproproteins in the purple bacterium R ubrivivax gelatinosus ; herein, we show that CopA is not directly required for cytochrome c oxidase but is vital for copper tolerance. Interestingly, excess copper in the copA − mutant resulted in a substantial decrease of the cytochrome c oxidase and the photosystem under microaerobic and anaerobic conditions together with the extrusion of coproporphyrin III . The data indicated that copper targeted the tetrapyrrole biosynthesis pathway at the level of the coproporphyrinogen III oxidase HemN and thereby affects the oxidase and the photosystem. This is the first in vivo demonstration that copper, like oxygen, affects tetrapyrrole biosynthesis presumably at the level of the SAM and [ 4Fe‐4S ] containing HemN enzyme. In light of these results and similar findings in E scherichia coli , the potential role of copper ions in the evolution of [ 4Fe‐4S ] enzymes and the Cu + ‐ ATPases is discussed.