Mercaptoethanesulfonic acid

Allen JR, DD Clark, JG Krumn, SA Ensign (1999) A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc Natl Acad Sci USA 96 8432-8437. 

Reconstruction of Au(lll) is observed in STM images as double rows separated from each other by 6.3 nm [335]. Some model calculations have been performed [362] to show that the energy difference of the reconstructed and unreconstructed Au(lll) is small. The effect of Triton X-100 on the reconstruction process of Au(lll) surface has been studied in chloride media [363] applying CV and double potential-step chronocoulometry. It has been found that adsorption of Triton X-100 stabilizes the reconstructed face of Au(lll). Hobara etal. [364] have used in situ STM to study reconstruction of Au(lll), following reductive desorption of 2-mercaptoethanesulfonic acid SAMs. 

Cysteic acid Sulphocysteine Phosphoserine Cysteine-2-mercaptoethanesulfonic acid disulfide... 

Zhou et al. studied the selective LbL assembly of NCs on microcontact printed carboxylate-functionalized SAMs.91 The LbL assembly was achieved by alternating adsorption of NCs functionalized with hydrophobic trioctylphosphine oxide and 2-mercaptoethanesulfonic acid, and positively charged linear poly(ethyleneimine) (LPEI). By adsorption of 11-mercaptoundecylhexa(ethylene glycol) in the noncon-tacted areas, nonspecific interactions were minimized. A uniform and linear growth of the polymer-NC layers was observed. 

Coenzyme M (CoM), 2-mercaptoethanesulfonic acid, was the first novel methanogen coenzyme described, and is the smallest organic coenzyme found in biological systems. The structure (Fig. 3) arose from work by Taylor, McBride, and Wolfe on methane production by extracts of Methanobacterium strain MOH, where a component was... 

Methylcobalamin also participates as a substrate for an enzymatic reaction in the formation of methane in certain methanogenic bacteria. In this reaction, which can be considered as a model for the second half-reaction of methionine synthetase, the cobalt-bound methyl group is transferred to 2-mercaptoethanesulfonic acid (coenzyme M) [39], the 5-methyl sulfide of which is subsequently reduced to yield methane. Additionally, methylcobalamin participates in the rather obscure process of acetate synthesis in certain bacteria in which it can be shown that the cobalt-bound methyl group becomes the acetate methyl carbon. The details of the involvement of methylcobalamin in this process are, however, unknown. 

Gulppi, M., S. Griveau, F. Bedioui, and J.H. Zagal (2001). Electrocatalysis of 2-mercaptoethanesulfonic acid oxidation on cobalt phthalocyanine modified elec-... 

Griveau, S., M. Gnlppi, J. Pavez, J.H. Zagal, and F. Bedioui (2003). Cobalt phthalocyanine-based molecular materials for the electrocatalysis and electroanalysis of 2-mercaptoethanol, 2-mercaptoethanesulfonic acid, reduced glutathione and L-cysteine. Electmancdysis 15(9), 779—785. 

The electrocatalytic oxidation of several thiols (2-mercaptoethanol, L-cysteine, glutathione and 2-mercaptoethanesulfonic acid) was studied using modified ultramicroelectrodes (UMEs) with poly-Co(II)-2 to allow further detection of thiols in micro-environment such as biological cells [54]. The modified UMEs were active toward the electro-oxidation of thiols in alkaline media, as shown on Fig. 18, with an electrocatalytic peak observed at ca -0.2 V/SCE for all the thiols studied. Their analytical performances toward cysteine and glutathione assessed by differential pulse amperometry are summarized in Tables 1 and 2. 

---