The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex
Abstract
Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes.
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Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Vásquez-Vivar, J., Kalyanaraman, B., Martásek, P., Hogg, N., Masters, B. S. S., Karoui, H., Tordo, P., & Pritchard, K. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9220 · Cited by 1,484
SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
Evans, S. V. (1993) · Journal of Molecular Graphics · doi:10.1016/0263-7855(93)87009-t · Cited by 1,279
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins
Solomon, E. I., Chen, P., Metz, M., Lee, S.-K., & Palmer, A. E. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20011217)40:24<4570::aid-anie4570>3.0.co;2-4 · Cited by 836
Mechanism of C-terminal amide formation by pituitary enzymes
Bradbury, A. F., Finnie, M. D. A., & Smyth, D. G. (1982) · Nature · doi:10.1038/298686a0 · Cited by 659
The Biosynthesis of Neuropeptides: Peptide alpha-Amidation
Eipper, B. A., Stoffers, D. A., & Mains, R. E. (1992) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.15.030192.000421 · Cited by 608
Self-citationMetalloenzymes, Structural Motifs, and Inorganic Models
Karlin, K. D. (1993) · Science · doi:10.1126/science.7688141 · Cited by 554
The Biosynthesis Of Neuropeptides: Peptide Alpha-Amidation
Eipper, B. (1992) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.15.1.57 · Cited by 488
Self-citationNew insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
Prigge, S. T., Mains, R. E., Eipper, B. A., & Amzel* **, L. M. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000763 · Cited by 460
Self-citationKinetics and Thermodynamics of Copper(I)/Dioxygen Interaction
Karlin, K. D., Kaderli, S., & Zuberbühler, A. D. (1997) · Accounts of Chemical Research · doi:10.1021/ar950257f · Cited by 409
Amidation of Bioactive Peptides: The Structure of Peptidylglycine α-Hydroxylating Monooxygenase
Prigge, S. T., Kolhekar, A. S., Eipper, B. A., Mains, R. E., & Amzel, L. M. (1997) · Science · doi:10.1126/science.278.5341.1300 · Cited by 353
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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
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
Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function
Adam, S. M., Wijeratne, G. B., Rogler, P. J., Diaz, D. E., Quist, D. A., Liu, J. J., & Karlin, K. D. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00074 · Cited by 264
Bousquet‐Moore, D., Mains, R. E., & Eipper, B. A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22404 · Cited by 66
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Metadata
- Authors
- Prigge, S. T., Eipper, B. A., Mains, R. E., & Amzel, L. M.
- Venue
- Science
- Published
- 2004-05-07
- Volume
- 304
- Issue
- 5672
- Pages
- 864-867
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1970713347
- Cited by
- 419
- References
- 28
- FWCI
- 20.26
- Type
- journal article
- Language
- en
- Open access
- closed
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