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Electronic structure contributions to function in bioinorganic chemistry
Abstract
Many metalloenzymes exhibit distinctive spectral features that are now becoming well understood. These reflect active site electronic structures that can make significant contributions to catalysis. Copper proteins provide well-characterized examples in which the unusual electronic structures of their active sites contribute to rapid, long-range electron transfer reactivity, oxygen binding and activation, and the multielectron reduction of dioxygen to water.
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Cited by
Electron transfer and reaction mechanism of laccases
Jones, S. M., & Solomon, E. I. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1826-6 · Cited by 623
Self-citationBerks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596
Olivares, C., & Solano, F. (2009) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2009.00636.x · Cited by 312
Tyrosinase Autoactivation and the Chemistry of ortho-Quinone Amines
Land, E. J., Ramsden, C. A., & Riley, P. A. (2003) · Accounts of Chemical Research · doi:10.1021/ar020062p · Cited by 169
Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues
Novotny, W. F., Chassande, O., Baker, M., Lazdunski, M., & Barbry, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36970-3 · Cited by 93
Metadata
- Authors
- Solomon, E., & Lowery, M.
- Venue
- Science
- Published
- 1993-03-12
- Volume
- 259
- Issue
- 5101
- Pages
- 1575-1581
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2067623205
- Cited by
- 411
- References
- 0
- FWCI
- 19.35
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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