期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 57, 期 39, 页码 12754-12758出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201807366
关键词
bioinorganic chemistry; metalloenzymes; two-color techniques; valence-to-core; X-ray emission spectroscopy
资金
- National Institutes of Health for National Research Service Awards [GM113389-01, GM116353-01]
- National Science Foundation Graduate Research Fellowship Program [DGE1255832]
- National Institutes of Health [GM55365]
- National Science Foundation [DMR-1332208]
Proton transfer reactions are of central importance to a wide variety of biochemical processes, though determining proton location and monitoring proton transfers in biological systems is often extremely challenging. Herein, we use two-color valence-to-core X-ray emission spectroscopy (VtC XES) to identify protonation events across three oxidation states of the O-2-activating, radical-initiating manganese-iron heterodinuclear cofactor in a class I-c ribonucleotide reductase. This is the first application of VtC XES to an enzyme intermediate and the first simultaneous measurement of two-color VtC spectra. In contrast to more conventional methods of assessing protonation state, VtC XES is a more direct probe applicable to a wide range of metalloenzyme systems. These data, coupled to insight provided by DFT calculations, allow the inorganic cores of the (MnFeIV)-Fe-IV and (MnFeIII)-Fe-IV states of the enzyme to be assigned as Mn-IV(-O)(2)Fe-IV and Mn-IV(-O)(-OH)Fe-III, respectively.
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