The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Copper Proteins and Copper Enzymes
Abstract
The copper proteins that function in homeostasis, electron transport, dioxygen transport and oxidation are discussed. Particular emphasis is placed on the role of the ligands, their type and disposition which, in conjunction with other residues in the active site, determine the role of the copper ion. It is proposed that copper proteins can be considered in four groups. Those in Group I contain a single copper ion in an approximately tetrahedral environment with nitrogen and sulphur-containing ligands. Group II proteins have a single copper ion in a square-planar-like arrangement. Group III proteins have two copper ions in close proximity. Group IV consists of multi-copper proteins, composed of sites representative of the other three groups.
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Cites
Stability constants of metal-ion complexes
Sillén, L. G., Martell, A. E., Bjerrum, J., & Schwarzenbach, G. (1964) · Medical Entomology and Zoology · Cited by 3,983
Fridovich, I. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001051 · Cited by 1,730
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X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution
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Molecular Mechanisms of Oxygen Activation
GEARY, P. J. (1975) · Biochemical Society Transactions · doi:10.1042/bst0030218a · Cited by 570
Copper chelates as possible active forms of the antiarthritic agents
Sorenson, J. R. J. (1976) · Journal of Medicinal Chemistry · doi:10.1021/jm00223a024 · Cited by 509
Richardson, J., Thomas, K. A., Rubin, B. H., & Richardson, D. C. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.4.1349 · Cited by 403
A crystallographic model for azurin at 3 Å resolution
Adman, E. T., Stenkamp, R. E., Sieker, L. C., & Jensen, L. H. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90375-3 · Cited by 351
On the Stability of Bovine Superoxide Dismutase
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Cited by
Halaouli, S., Asther, M., Sigoillot, J.-C., Hamdi, M., & Lomascolo, A. (2006) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2006.02866.x · Cited by 359
Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274
Welch, K. D., Davis, T. Z., Van Eden, M. E., & Aust, S. D. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00760-8 · Cited by 205
Role of Ceruloplasmin in Macrophage Iron Efflux during Hypoxia
Sarkar, J., Seshadri, V., Tripoulas, N. A., Ketterer, M. E., & Fox, P. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304926200 · Cited by 101
Metadata
- Authors
- Cass, A. E. G., & Hill, H. A. O.
- Venue
- Novartis Foundation Symposia
- Publisher
- Wiley
- Published
- 1980-01
- Volume
- 79
- Pages
- 71-91
- ISSN
- 1528-2511 (ISSN-L)
- 1935-4657
- OpenAlex
- W1589521344
- Cited by
- 290
- References
- 23
- Type
- other
- Language
- en
- Open access
- closed
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
