How the Larger Methionine-Rich Domain of CueO from Hafnia alvei Enhances Cuprous Oxidation

CueOs, members of the multicopper oxidase family, play a crucial role in bacterial copper detoxification. These enzymes feature a unique methionine-rich (Met-rich) domain, which is essential for the oxidation of Cu+ to Cu2+. Recent studies using CueO fro...

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المؤلف الرئيسي:	Umberto Contaldo (4438690) (author)
مؤلفون آخرون:	Paolo Santucci (21072356) (author), Alexandra Vergnes (3286863) (author), Philippe Leone (11068354) (author), Jérôme Becam (21072359) (author), Frédéric Biaso (2102212) (author), Marianne Ilbert (578410) (author), Benjamin Ezraty (3286860) (author), Elisabeth Lojou (578408) (author), Ievgen Mazurenko (2194315) (author)
منشور في:	2025
الموضوعات:	Biochemistry Microbiology Cell Biology Genetics Ecology Sociology Environmental Sciences not elsewhere classified providing new insights multicopper oxidase family enhanced activity correlates detailed structural basis demonstrating superior efficiency cuprous oxidase activity highly chelated species hafnia alvei </ escherichia coli </ higher methionine content free electrogenerated cu bacterial copper detoxification chelation strength increases weakly chelated cu sup >+</ sup significantly larger met role becomes crucial copper detoxification larger methionine chelation strength chelated forms ha </ ec </ crucial role unique methionine stronger chelation oxidizing cu facilitating cu different cu variant lacking ray crystallography quantified either pivotal role molecular dynamics methods enabled first showed enzymes feature comparative analyses
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How the Larger Methionine-Rich Domain of CueO from <i>Hafnia alvei</i> Enhances Cuprous Oxidation

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