期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 141, 期 37, 页码 14510-14514出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b06093
关键词
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资金
- National Science Foundation [CHE-1610676]
- National Institutes of Health (National Research Service) [GM 116353, GM-103220]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences
- DOE Office of Science [DE-AC02-06CH11357]
- National Cancer Institute [ACB-12002]
- National Institute of General Medical Sciences [AGM -12006]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor Grant [085P1000817]
The iron-dependent oxidase UndA cleaves one C3-H bond and the C1-C2 bond of dodecanoic acid to produce 1-undecene and CO2. A published X-ray crystal structure showed that UndA has a heme-oxygenase-like fold, thus associating it with a structural superfamily that includes known and postulated non-heme diiron proteins, but revealed only a single iron ion in the active site. Mechanisms proposed for initiation of decarboxylation by cleavage of the C3-H bond using a monoiron cofactor to activate O-2 necessarily invoked unusual or potentially unfeasible steps. Here we present spectroscopic, crystallographic, and biochemical evidence that the cofactor of Pseudomonas fluorescens Pf-S UndA is actually a diiron cluster and show that binding of the substrate triggers rapid addition of O-2 to the Fe-2(II/II) cofactor to produce a transient peroxo-Fe-2(III/III) intermediate. The observations of a diiron cofactor and substrate-triggered formation of a peroxo-Fe-2(III/III) intermediate suggest a small set of possible mechanisms for O-2, C3-H and C1-C2 activation by UndA; these routes obviate the problematic steps of the earlier hypotheses that invoked a single iron.
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