Cited by 243Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionMetal-Catalyzed Oxygenation Mechanisms

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A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes

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Huber, R, Hof, P, Duarte, R O, Moura, J J, Moura, I, Liu, M Y, LeGall, J, Hille, R, Archer, M, Romão, M J·1996·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.93.17.8846PMC PMC38556

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Abstract

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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Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
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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)
ORCID: Huber, R
Moura, J J
Moura, I
Hille, R
Archer, M
Romão, M J
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
DOI: 10.1073/pnas.93.17.8846
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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A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes

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