The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Side-On Copper-Nitrosyl Coordination by Nitrite Reductase
Abstract
A copper-nitrosyl intermediate forms during the catalytic cycle of nitrite reductase, the enzyme that mediates the committed step in bacterial denitrification. The crystal structure of a type 2 copper-nitrosyl complex of nitrite reductase reveals an unprecedented side-on binding mode in which the nitrogen and oxygen atoms are nearly equidistant from the copper cofactor. Comparison of this structure with a refined nitrite-bound crystal structure explains how coordination can change between copper-oxygen and copper-nitrogen during catalysis. The side-on copper-nitrosyl in nitrite reductase expands the possibilities for nitric oxide interactions in copper proteins such as superoxide dismutase and prions.
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Cites
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Nitric oxide : biology and pathobiology
Ignarro, L. J. (2000) · Cited by 1,306
Estévez, A. G., Crow, J. P., Sampson, J. B., Reiter, C., Zhuang, Y., Richardson, G. J., Tarpey, M. M., Barbeito, L., & Beckman, J. S. (1999) · Science · doi:10.1126/science.286.5449.2498 · Cited by 596
Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron
Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., & Ramaswamy, S. (2003) · Science · doi:10.1126/science.1078020 · Cited by 560
Dissimilatory Nitrite and Nitric Oxide Reductases
Averill, B. A. (1996) · Chemical Reviews · doi:10.1021/cr950056p · Cited by 544
Wasser, I. M., de Vries, S., Moënne-Loccoz, P., Schröder, I., & Karlin, K. D. (2002) · Chemical Reviews · doi:10.1021/cr0006627 · Cited by 476
The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from Achromobacter cycloclastes
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Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
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Cited by
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M., Kieber-Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,751
The emerging biology of the nitrite anion
Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609
Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control
Huang, Z. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24650 · Cited by 520
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Metadata
- Authors
- Tocheva, E. I., Rosell, F. I., Mauk, A. G., & Murphy, M. E. P.
- Venue
- Science
- Published
- 2004-05-07
- Volume
- 304
- Issue
- 5672
- Pages
- 867-870
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2045547222
- Cited by
- 253
- References
- 31
- FWCI
- 16.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tocheva, E. I., Rosell, F. I., Mauk, A. G., & Murphy, M. E. P. (2004). Side-On Copper-Nitrosyl Coordination by Nitrite Reductase. Science. https://doi.org/10.1126/science.1095109
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
