The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S -selanylcysteine
Open accessAbstract
CO dehydrogenase from the aerobic bacterium Oligotropha carboxidovorans catalyzes the oxidation of CO with H 2 O, yielding CO 2 , two electrons, and two H + . Its crystal structure in the air-oxidized form has been determined to 2.2 Å. The active site of the enzyme, which contains molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S -selanylcysteine, delivers the electrons to an intramolecular electron transport chain composed of two types of [2Fe–2S] clusters and flavin-adenine dinucleotide. CO dehydrogenase is composed of an 88.7-kDa molybdoprotein (L), a 30.2-kDa flavoprotein (M), and a 17.8-kDa iron-sulfur protein (S). It is organized as a dimer of LMS heterotrimers and resembles xanthine dehydrogenase/oxidase in many, but not all, aspects. A mechanism based on a structure with the bound suicide-substrate cyanide is suggested and displays the necessity of S -selanylcysteine for the catalyzed reaction.
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Cites
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,953
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
de La Fortelle, E., & Bricogne, G. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76073-7 · Cited by 1,892
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
Selenium reagents and intermediates in organic synthesis
Paulmier, C. (1986) · Cited by 881
Microbial growth on C[1] compounds
Murrell, J. C., & Kelly, D. P. (1993) · Intercept eBooks · Cited by 493
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., Schneider, M., Hof, P., & Huber, R. (1995) · Science · doi:10.1126/science.270.5239.1170 · Cited by 480
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The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Reich, H. J., & Hondal, R. J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00031 · Cited by 923
Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733
Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution
Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R., & Meyer, O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212640899 · Cited by 386
Self-citationGreat Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
Metadata
- Authors
- Dobbek, H., Gremer, L., Meyer, O., & Huber, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-08-03
- Volume
- 96
- Issue
- 16
- Pages
- 8884-8889
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1991180369
- Cited by
- 254
- References
- 26
- FWCI
- 21.41
- Type
- journal article
- Language
- en
- Open access
- green
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- Dobbek, H., Gremer, L., Meyer, O., & Huber, R. (1999). Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S -selanylcysteine. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.16.8884
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