NDLI: Structure and stability of the molybdenum cofactor intermediate cyclic pyranopterin monophosphate.

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Structure and stability of the molybdenum cofactor intermediate cyclic pyranopterin monophosphate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Santamaria-Araujo, Jose Angel Wray, Victor Schwarz, Guenter
Description	Country affiliation: Germany Author Affiliation: Santamaria-Araujo JA ( Institute of Biochemistry, Department of Chemistry & Center for Molecular Medicine Cologne, University of Cologne, 50674 Cologne, Germany. santamaria.araujo@gmail.com)
Abstract	Hydrogenated (reduced) pterins are found in all living organisms, where they are involved in key metabolic processes. Molybdenum in its biologically active form is bound to a fully reduced tetrahydropyranopterin referred to as a metal-binding pterin (MPT), forming the so-called molybdenum cofactor (Moco). Cyclic pyranopterin monophosphate (cPMP) is the first isolatable intermediate in molybdenum cofactor biosynthesis. Here we present for the first time a (13)C NMR characterization of an active Moco intermediate. The (13)C NMR data for cPMP corroborate previous data showing the tetrahydropyranopterin nature of cPMP and the presence of a gem-diol in the C1' position of the side chain. The stability of the gem-diol, together with the absence of any observable signal at low field (175-220 ppm), is an indication that the gem-diol is not a chemical artifact, but is chemically stable and not in equilibrium with the keto form. Finally, we have studied spectrophotometrically the kinetics of cPMP oxidation in the presence of metal centers, chelating agents, and different buffers and pH values. We found that oxidation is metal-dependent and can be substantially retarded in the presence of EDTA.
File Format	HTM / HTML
ISSN	09498257
Issue Number	1
Volume Number	17
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2012-01-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Coenzymes Chemistry Metalloproteins Organophosphorus Compounds Pteridines Pterins Metabolism Kinetics Magnetic Resonance Spectroscopy Molecular Structure Isolation & Purification Oxidation-reduction Protein Stability Spectrophotometry, Ultraviolet Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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