van Staalduinen, Laura M.;
McSorley, Fern R.;
Schiessl, Katharina;
Séguin, Jacqueline;
Wyatt, Peter B.;
Hammerschmidt, Friedrich;
Zechel, David L.;
Jia, Zongchao
Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates
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Medientyp:
E-Artikel
Titel:
Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates
Beteiligte:
van Staalduinen, Laura M.;
McSorley, Fern R.;
Schiessl, Katharina;
Séguin, Jacqueline;
Wyatt, Peter B.;
Hammerschmidt, Friedrich;
Zechel, David L.;
Jia, Zongchao
Erschienen:
Proceedings of the National Academy of Sciences, 2014
Erschienen in:
Proceedings of the National Academy of Sciences, 111 (2014) 14, Seite 5171-5176
Sprache:
Englisch
DOI:
10.1073/pnas.1320039111
ISSN:
0027-8424;
1091-6490
Entstehung:
Anmerkungen:
Beschreibung:
Significance Inorganic phosphate (Pi) is an essential component of many biological molecules and thus is required by all life forms. However, soluble Pi is typically at low abundance in the environment. To compensate, microbes have evolved unique carbon–phosphorus-bond cleaving reactions to use organophosphonates as an alternative source of Pi. The marine-derived enzyme PhnZ utilizes a new oxidative mechanism for CP bond cleavage involving iron and molecular oxygen. The three-dimensional structure of PhnZ reveals unique active site features that contribute to catalysis of CP bond cleavage and substrate specificity, as well as an evolutionary link between phosphodiester bond hydrolysis and oxidative bond cleavage. This evolutionary link likely reflects the ancient origins of organophosphonates in the environment.