NDLI: Resonance Raman as a direct probe for the catalytic mechanism of molybdenum oxotransferases

Content Provider	Springer Nature Link
Author	Johnson, M. K. Garton, Shann D. Oku, Hiroyuki
Copyright Year	1997
Abstract	Recent studies of human sulfite oxidase and Rhodobacter sphaeroides DMSO reductase have demonstrated the ability of resonance Raman to probe in detail the coordination environment of the Mo active sites in oxotransferases via Mo=O, Mo-S(dithiolene), Mo-S(Cys) or Mo-O(Ser), dithiolene chelate ring and bound substrate vibrations. Furthermore, the ability to monitor the catalytically exchangeable oxo group via isotopic labeling affords direct mechanistic information and structures for the catalytically competent Mo(IV) and Mo(VI) species. The results clearly demonstrate that sulfite oxidase cycles between cis–di-oxo-Mo(VI) and mono-oxo-Mo(IV) states during catalytic turnover, whereas DMSO reductase cycles between mono-oxo-Mo(VI) and des-oxo-Mo(IV) states. In the case of DMSO reductase, 18O-labeling experiments have provided the first direct evidence for an oxygen atom transfer mechanism involving an Mo=O species. Of particular importance is that the active-site structures and detailed mechanism of DMSO reductase in solution, as determined by resonance Raman spectroscopy, are quite different to those reported or deduced in the three X-ray crystallographic studies of DMSO reductases from Rhodobacter species.
Starting Page	797
Ending Page	803
Page Count	7
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	2
Issue Number	6
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	1997-12-17
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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