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A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes
Open accessAbstract
The crystal structure of the xanthine oxidase-related molybdenum-iron protein aldehyde oxido-reductase from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas (Mop) was analyzed in its desulfo-, sulfo-, oxidized, reduced, and alcohol-bound forms at 1.8-A resolution. In the sulfo-form the molybdenum molybdopterin cytosine dinucleotide cofactor has a dithiolene-bound fac-[Mo, = O, = S, ---(OH2)] substructure. Bound inhibitory isopropanol in the inner compartment of the substrate binding tunnel is a model for the Michaelis complex of the reaction with aldehydes (H-C = O,-R). The reaction is proposed to proceed by transfer of the molybdenum-bound water molecule as OH- after proton transfer to Glu-869 to the carbonyl carbon of the substrate in concert with hydride transfer to the sulfido group to generate [MoIV, = O, -SH, ---(O-C = O, -R)). Dissociation of the carboxylic acid product may be facilitated by transient binding of Glu-869 to the molybdenum. The metal-bound water is replenished from a chain of internal water molecules. A second alcohol binding site in the spacious outer compartment may cause the strong substrate inhibition observed. This compartment is the putative binding site of large inhibitors of xanthine oxidase.
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“It catalyzes the oxidation of the bases hypoxanthine and xanthine to uric acid, which is the end product of purine catabolism. H2O2 is generated as a byproduct during two oxidation steps of the enzymatic reaction, marking XO as a potential ROS source.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [139]
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Metadata
- Authors
- Huber, R., Hof, P., Duarte, R. O., Moura, J. J., Moura, I., Liu, M. Y., LeGall, J., Hille, R., Archer, M., & Romão, M. J.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1996-08-20
- Volume
- 93
- Issue
- 17
- Pages
- 8846-8851
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC38556
- OpenAlex
- W2057637394
- Cited by
- 242
- References
- 37
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 6 · 2022: 5 · 2021: 6 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 8 · 2016: 7 · 2015: 8 · 2014: 12 · 2013: 6 · 2012: 6
- FWCI
- 22.24
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- xanthine oxidase, molybdenum enzymes, aldehyde oxidase, Desulfovibrio gigas, molybdenum-iron protein, molybdopterin, catalytic mechanism, hydride transfer, crystal structure
- MeSH terms
- Aldehyde Oxidoreductases, Bacterial Proteins, Cytosine Nucleotides, Desulfovibrio, Models, Molecular, Molybdenum, Oxidation-Reduction, Pterins, Xanthine Oxidase, Crystallography, X-Ray
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