Biothiols, Part A: Monothiols and Dithiols, Protein Thiols, by John N. Abelson, Melvin I. Simon, Helmut Sies

By John N. Abelson, Melvin I. Simon, Helmut Sies

The seriously acclaimed laboratory regular for 40 years, Methods in Enzymology is likely one of the so much hugely revered guides within the box of biochemistry. when you consider that 1955, every one quantity has been eagerlyawaited, often consulted, and praised via researchers and reviewers alike. greater than 250 volumes were released (all of them nonetheless in print) and lots more and plenty of the fabric is appropriate even today--truly a vital e-book for researchers in all fields of existence sciences. Key good points * Prevention of oxidative pressure * Redox rules of metabolism * Toxicology * Carcinogenesis

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Extra info for Biothiols, Part A: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals

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1). 27 Efficient catalysis is often associated with internal equilibrium constants that are close to one. 28 For lipoyl dehydrogenase, however, the redox potential for transfer of the first two electrons (presumably the dithiol/disulfide center) is 66 mV more negative than that for transfer of the next two electrons (presumably the flavin), suggesting a favorable transfer of electrons from the dithiol center to the flavin. 29 Magnitude of Thiol/Disulfide Redox Equilibrium Constants Mixed Disulfides For alkyl thiols such as the cysteine residues of most proteins, the equilibrium constants for mixed disulfide formation are usually near one (Table I).

Soc. 102, 2011 (1980). 10 OVERVIEW , [2] If the test system has two sulfhydryl groups that are in close enough proximity, the initially formed mixed disulfide may be displaced by an intramolecular reaction leading to the formation of an intramolecular disulfide. While the overall reaction is complicated by the potential accumulation of multiple redox isomers (see Complex Equilibria), in practice, the intramolecular reaction is often so favorable that negligible mixed disulfide species are present at equilibrium.

Grimsley, J. A. Thomson, and B. J. Barnett, J. Biol. Chem. 263,11820 (1988). 12 OVERVIEW ' [21 In small peptides and unfolded proteins, the thiol/disulfide oxidation potential depends on the sequence distance between the two cysteine residues. Because of geometric constraints, the most stable disulfide bond is formed by residues that have four to five intervening residues and decreases further as the intervening number of amino acids increases. 1 M. In folded proteins, Kox may approach 105 M J The larger the ratio of Kox for the folded protein to that of the unfolded protein, the greater the stability of the disulfide-cross-linked protein compared to that of the reduced protein.

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