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A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes
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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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Cites
Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R. A., Schneider, M., Hof, P., & Huber, R. (1995) · Science · doi:10.1126/science.270.5239.1170 · Cited by 481
Self-citationOn the Mechanism of Inactivation of Xanthine Oxidase by Cyanide
Massey, V., & Edmondson, D. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62575-x · Cited by 368
Grams, F., Reinemer, P., Powers, J. C., Kleine, T., Pieper, M. P., Tschesche, H., Huber, R., & Bode, W. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20329.x · Cited by 180
Self-citationThe inorganic biochemistry of molybdoenzymes
Bray, R. C. (1988) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500004479 · Cited by 160
Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases.
Wahl, R. C., & Rajagopalan, K. V. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68199-8 · Cited by 143
Active site topology and reaction mechanism of GTP cyclohydrolase I.
Nar, H., Huber, R., Auerbach, G., Fischer, M. J., Hoesl, C. E., Ritz, H., Bracher, A., Meining, W., Eberhardt, S., & Bacher, A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12120 · Cited by 125
Self-citationGutteridge, S., Tanner, S. J., & Bray, R. C. (1978) · Biochemical Journal · doi:10.1042/bj1750887 · Cited by 125
Arginine 127 stabilizes the transition state in carboxypeptidase
Phillips, M. A., Fletterick, R. J., & Rutter, W. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30559-8 · Cited by 119
Three-dimensional structure of porcine pancreatic procarboxypeptidase A
Guasch, A., Coll, M., Avilés, F. X., & Huber, R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90581-4 · Cited by 114
Self-citationHille, R., & Sprecher, H. W. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60902-0 · Cited by 113
Self-citation
Flagged first, then by citations
Research works printed but not linked: 7
- Brunger, A. T. (1990) X-PLOR Version 2.1 Manual (Yale Univ. Press, New Haven, CT).
- Reuben, J. & Berliner, L. J. (Plenum, New York), Vol. 2, pp. 45-84.
- Tanner, S. J. & Bray, R. C. (1978) Biochem. Soc. Trans. 6, 1331-1333.
- Hille, R. & Massey, V. (1985) in Molybdenum Enzymes, ed. Spiro, T. G. (Wiley, New York), pp. 443-518.
- Bray, R. C. & George, G. N. (1985) Biochem. Soc. Trans. 13, 560-567.
- Bray, R. C. (1980) in Biological Magnetic Resonance, eds. Berliner, L. J. & Reuben, J. (Plenum, New York), Vol. 2, pp. 45-84.
- Nar, H., Huber, R., Auerbach, G., Fischer, R., H6sl, C., Ritz, H., Bracher, A., Meining, W., Eberhardt, S. & Bacher, A.(1995) Proc. Natl. Acad. Sci. USA 92, 12120-12125.
Cited by
Sorted by citations
Items 101–200 of 243
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Hagen, W. R., & Arendsen, A. F. (1998) · Structure and bonding · doi:10.1007/3-540-62888-6_6 · Cited by 40
Foti, A., Hartmann, T., Coelho, C., Santos‐Silva, T., Romão, M. J., & Leimkühler, S. (2016) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.068395 · Cited by 39
Self-citationCosper, M. M., Neese, F., Astashkin, A. V., Carducci, M. D., Raitsimring, A. M., & Enemark, J. H. (2005) · Inorganic Chemistry · doi:10.1021/ic0483850 · Cited by 39
Boer, R., Thapper, A., Brondino, C. D., Romão, M. J., & Moura, J. J. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0490222 · Cited by 38
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Hille, R., & Anderson, R. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100673200 · Cited by 38
Self-citationVoityuk, A. A., Albert, K., Gemming, S., Nasluzov, V. A., Neyman, K. M., Hof, P., Huber, R., Romão, M. J., & Rösch, N. (1997) · Journal of the American Chemical Society · doi:10.1021/ja963901+ · Cited by 38
Self-citationReductive Half-Reaction of Aldehyde Oxidoreductase toward Acetaldehyde: A Combined QM/MM Study
Metz, S., Wang, D., & Thiel, W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja805938w · Cited by 37
A new aldehyde oxidase selectively expressed in chemosensory organs of insects
Merlin, C., François, M., Bozzolan, F., Pelletier, J., Jacquin‐Joly, E., & Maı̈bèche, M. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.084 · Cited by 37
Synthesis and reactivity studies of model complexes for molybdopterin-dependent enzymes
Thapper, A., Lorber, C. Y., Fryxelius, J., Behrens, A., & Nordlander, E. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00010-6 · Cited by 37
Ilich, P., & Hille, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja011957k · Cited by 36
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Zanello, P. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.08.003 · Cited by 35
Partyka, D. V., & Holm, R. H. (2004) · Inorganic Chemistry · doi:10.1021/ic040097g · Cited by 35
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Structure and function of the xanthine-oxidase family of molybdenum enzymes
Romão, M. J., & Huber, R. (1998) · Structure and bonding · doi:10.1007/3-540-62888-6_3 · Cited by 34
Self-citationOku, H., Ueyama, N., & Nakamura, A. (1997) · Inorganic Chemistry · doi:10.1021/ic951277g · Cited by 33
Electronic Spectral Studies of Molybdenyl Complexes. 2. MCD Spectroscopy of [MoOS4]- Centers
McMaster, J., Carducci, M. D., Yang, Y., Solomon, E. I., & Enemark, J. H. (2001) · Inorganic Chemistry · doi:10.1021/ic0005846 · Cited by 33
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Wells, M., Kim, M., Akob, D. M., Basu, P., & Stolz, J. F. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.04145-22 · Cited by 33
QM/MM Studies of Xanthine Oxidase: Variations of Cofactor, Substrate, and Active-Site Glu802
Metz, S., & Thiel, W. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp909999s · Cited by 32
Santos‐Silva, T., Ferroni, F. M., Thapper, A., Marangon, J., González, P. J., Rizzi, A. C., Moura, I., Moura, J. J. G., Romão, M. J., & Brondino, C. D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809448r · Cited by 33
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Trager, W. F. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00119-x · Cited by 32
Sekine, M., Okamoto, K., & Ichida, K. (2021) · Biomedicines · doi:10.3390/biomedicines9111723 · Cited by 31
Metalloproteins/metalloenzymes for the synthesis of acetyl-CoA in the Wood-Ljungdahl pathway
Zhu, X., & Tan, X. (2009) · Science China Chemistry · doi:10.1007/s11426-009-0082-3 · Cited by 29
Liao, R., Yu, J., & Himo, F. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.03.020 · Cited by 29
Carrano, C. J., Chohan, B. S., Hammes, B. S., Kail, B. W., Nemykin, V. N., & Basu, P. (2003) · Inorganic Chemistry · doi:10.1021/ic0262785 · Cited by 29
Akram, M., Bhat, I. A., Bhat, W. F., & KABIR‐UD‐DIN, K. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.05.056 · Cited by 30
Interaction of a green ester-bonded gemini surfactant with xanthine oxidase: Biophysical perspective
Akram, M., Bhat, I. A., & KABIR‐UD‐DIN, K. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.03.050 · Cited by 28
Glatigny, A., Hof, P., Romão, M. J., Huber, R., & Scazzocchio, C. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1707 · Cited by 28
Self-citationEierhoff, D., Tung, W. C., Hammerschmidt, A., & Krebs, B. (2008) · Inorganica Chimica Acta · doi:10.1016/j.ica.2008.01.026 · Cited by 28
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Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K., & Uwajima, T. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00781-x · Cited by 27
Jalilehvand, F., Lim, B. S., Holm, R. H., Hedman, B., & Hodgson, K. O. (2003) · Inorganic Chemistry · doi:10.1021/ic030039f · Cited by 27
Periyasamy, G., Sundararajan, M., Hillier, I. H., Burton, N. A., & McDouall, J. J. W. (2007) · Physical Chemistry Chemical Physics · doi:10.1039/b701083d · Cited by 27
Biani, F. F. D., & Zanello, P. (2016) · Inorganica Chimica Acta · doi:10.1016/j.ica.2016.09.028 · Cited by 27
Pal, K., Chaudhury, P. K., & Sarkar, S. (2007) · Chemistry - An Asian Journal · doi:10.1002/asia.200700020 · Cited by 26
Inscore, F. E., Joshi, H., McElhaney, A. E., & Enemark, J. H. (2002) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(01)00817-9 · Cited by 25
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Wang, J., Keceli, G., Cao, R., Su, J., & Mi, Z. (2016) · Redox Report · doi:10.1080/13510002.2016.1206175 · Cited by 24
Dhawan, I. K., Roy, R., Koehler, B. P., Mukund, S., Adams, M. W. W., & Johnson, M. K. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/pl00010660 · Cited by 24
Reichenbecher, W., & Schink, B. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00004-7 · Cited by 24
Kaufmann, H. L., Liable‐Sands, L. M., Rheingold, A. L., & Burgmayer, S. J. N. (1999) · Inorganic Chemistry · doi:10.1021/ic980881z · Cited by 24
Kirk, M. L., & Stein, B. W. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00316-8 · Cited by 23
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Graff, J. N., McElhaney, A. E., Basu, P., Gruhn, N. E., Chang, C.-S. J., & Enemark, J. H. (2002) · Inorganic Chemistry · doi:10.1021/ic0110981 · Cited by 22
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Self-citationDopke, J. A., Wilson, S. R., & Rauchfuss, T. B. (2000) · Inorganic Chemistry · doi:10.1021/ic0001661 · Cited by 21
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Moura, I., Pereira, A. S., Tavares, P., & Moura, J. J. G. (1999) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60083-5 · Cited by 21
Self-citationChaves, S., Gil, M., Canário, S., Jelić, R., Romão, M. J., Trincão, J., Herdtweck, E., Sousa, J. B., Diniz, C., Fresco, P., et al. (2008) · Dalton Transactions · doi:10.1039/b717172b · Cited by 20
Self-citationJin, J., Straathof, A. J. J., Pinkse, M. W. H., & Hanefeld, U. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2996-2 · Cited by 19
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Wang, X., Inscore, F. E., Yang, X., Cooney, J. J. A., Enemark, J. H., & Wang, L. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0265557 · Cited by 19
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Stiefel, E. I., & Pilato, R. S. (1999) · CRC Press eBooks · doi:10.1201/9780203908457.ch6 · Cited by 19
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Pellei, M., Papini, G., Lobbia, G. G., & Santini, C. (2009) · Current Bioactive Compounds · doi:10.2174/157340709789816456 · Cited by 18
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Eagle, A. A., George, G. N., Tiekink, E. R. T., & Young, C. G. (1999) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(99)00106-3 · Cited by 15
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Duarte, R. O., Archer, M., Dias, J. M. L., Bursakov, S. A., Huber, R., Moura, I., Romão, M. J., & Moura, J. J. G. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2135 · Cited by 14
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Self-citationMota, C., Esmaeeli, M., Coelho, C., Santos‐Silva, T., Wolff, M., Foti, A., Leimkühler, S., & Romão, M. J. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12617 · Cited by 12
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Self-citationOku, H., Ueyama, N., & Nakamura, A. (1999) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.72.2261 · Cited by 11
Mirzaei, S., Taherpour, A. A., & Mohamadi, S. (2016) · RSC Advances · doi:10.1039/c6ra19197e · Cited by 10
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Self-citationMori, T., Masuzawa, N., Kondo, K., Nakanishi, Y. Y., Chida, S., Uehara, D., Katahira, M., & Takeda, M. (2022) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbac207 · Cited by 7
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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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