期刊
CHEMICAL RESEARCH IN TOXICOLOGY
卷 30, 期 3, 页码 729-762出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrestox.6b00428
关键词
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资金
- NIGMS [P41-GM103311]
The unique biophysical and electronic properties of cysteine make this molecule one of the most biologically critical amino acids in the proteome. The defining sulfur atom in cysteine is much larger than the oxygen and nitrogen atoms more commonly found in the other amino acids. As a result of its size, the valence electrons of sulfur are highly polarizable. Unique protein microenvironments favor the polarization of sulfur, thus increasing the overt reactivity of cysteite Here, we provide a brief overview of the endogenOus generation of reactive Oxygen and electrophilic species and specific examples of enzymes arid transcription factors in which the Oxidation or covalent modification of cysteine in those prOteins modulates their function. The perspective concludes with a discussion of cysteine chemistry and biophysics, the hard and soft acids and bases model, and the proposal of the Soft Cysteine Signaling Network: a hypothesis proposing the existence of a complex signaling network governed by layered chemical reactivity and cross-talk in which the chemical modification of reactive cysteine in biological networks triggers the reorganization of intracellular biochemistry to mitigate spikes in endogenous or exogenous oxidative or electrophilic stress.
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