The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Tyrosine Hydroxylase Is Inactivated by Catechol‐Quinones and Converted to a Redox‐Cycling Quinoprotein: Possible Relevance to Parkinson’s Disease
Abstract
Abstract Quinone derivatives of DOPA, dopamine, and N‐acetyldopamine inactivate tyrosine hydroxylase, the initial and rate‐limiting enzyme in the biosynthesis of the catecholamine neurotransmitters. The parent catechols are inert in this capacity. The effects of the catecholquinones on tyrosine hydroxylase are prevented by antioxidants and reducing reagents but not by scavengers of hydrogen peroxide, hydroxyl radicals, or superoxide radicals. Quinone modification of tyrosine hydroxylase modifies enzyme sulfhydryl groups and results in the formation of cysteinyl‐catechols within the enzyme. Catecholquinones convert tyrosine hydroxylase to a redox‐cycling quinoprotein. Quinotyrosine hydroxylase causes the reduction of the transition metals iron and copper and may therefore contribute to Fenton‐like reactions and oxidative stress in neurons. The discovery that a phenotypic marker for catecholamine neurons can be converted into a redox‐active species is highly relevant for neurodegenerative conditions such as Parkinson’s disease.
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Citations
Cites
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947
Oxidative Stress in Neurodegenerative Diseases
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Oxidative Pathways for Catecholamines in the Genesis of Neuromelanin and Cytotoxic Quinones
GRAHAM, D. G. (1978) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13535-9 · Cited by 1,126
The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
Fahn, S., & Cohen, G. (1992) · Annals of Neurology · doi:10.1002/ana.410320616 · Cited by 927
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739
Spencer, J. P. E., Jenner, P., Daniel, S. E., Lees, A. J., Marsden, D. C., & Halliwell, B. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71052112.x · Cited by 373
Long-lived reactive species on free-radical-damaged proteins
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Role of Endogenous Glutathione in the Oxidation of Dopamine
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Cited by
Oxidative stress and Parkinson’s disease
Blesa, J., Trigo-Damas, I., Quiroga-Varela, A., & Jackson-Lewis, V. R. (2015) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2015.00091 · Cited by 878
Role of Oxidative Stress in Parkinson's Disease
Hwang, O. (2013) · Experimental Neurobiology · doi:10.5607/en.2013.22.1.11 · Cited by 835
Asanuma, M., Miyazaki, I., & Ogawa, N. (2003) · Neurotoxicity Research · doi:10.1007/bf03033137 · Cited by 516
Oxidative stress and inflammation in Parkinson's disease: is there a causal link?
Hald, A., & Lotharius, J. (2005) · Experimental Neurology · doi:10.1016/j.expneurol.2005.01.013 · Cited by 508
Role of dopamine in the pathophysiology of Parkinson’s disease
Zhou, Z. D., Yi, L. X., Wang, D. Q., Lim, T. M., & Tan, E. K. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00378-6 · Cited by 308
Metadata
- Authors
- Kuhn, D. M., Arthur, R. E., Thomas, D. M., & Elferink, L. A.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1999-09
- Volume
- 73
- Issue
- 3
- Pages
- 1309-1317
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1781217464
- Cited by
- 183
- References
- 8
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kuhn, D. M., Arthur, R. E., Thomas, D. M., & Elferink, L. A. (1999). Tyrosine Hydroxylase Is Inactivated by Catechol‐Quinones and Converted to a Redox‐Cycling Quinoprotein: Possible Relevance to Parkinson’s Disease. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.1999.0731309.x
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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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