Dey, Mishtu published the artcileCharacterization of Alkyl-Nickel Adducts Generated by Reaction of Methyl-Coenzyme M Reductase with Brominated Acids, SDS of cas: 56523-59-2, the main research area is methyl coenzyme M reductase active site electron transfer.
Methyl-coenzyme M reductase (MCR) from methanogenic archaea catalyzes the final step in the biol. synthesis of methane. Using coenzyme B (CoBSH) as the two-electron donor, MCR reduces methyl-coenzyme M (methyl-SCoM) to methane and the mixed disulfide, CoB-S-S-CoM. MCR contains coenzyme F430, an essential redox-active nickel tetrahydrocorphin, at its active site. The active form of MCR (MCRred1) contains Ni(I)-F430. When 3-bromopropane sulfonate (BPS) is incubated with MCRred1, an alkyl-Ni(III) species is formed that elicits the MCRPS EPR signal. Here we used EPR and UV-visible spectroscopy and transient kinetics to study the reaction between MCR from Methanothermobacter marburgensis and a series of brominated carboxylic acids, with carbon chain lengths of 4-16. All of these compounds give rise to an alkyl-Ni intermediate with an EPR signal similar to that of the MCRPS species. Reaction of the alkyl-Ni(III) adduct, formed from brominated acids with eight or fewer total carbons, with HSCoM as nucleophile at pH 10.0 results in the formation of a thioether coupled to regeneration of the active MCRred1 state. When reacted with 4-bromobutyrate, MCRred1 forms the alkyl-Ni(III) MCRXA state and then, surprisingly, undergoes “”self-reactivation”” to regenerate the Ni(I) MCRred1 state and a bromocarboxy ester. The results demonstrate an unexpected reactivity and flexibility of the MCR active site in accommodating a broad range of substrates, which act as mol. rulers for the substrate channel in MCR.
Biochemistry published new progress about Electron donors. 56523-59-2 belongs to class bromides-buliding-blocks, name is 15-Bromopentadecanoic acid, and the molecular formula is C15H29BrO2, SDS of cas: 56523-59-2.
Referemce:
Bromide – Wikipedia,
bromide – Wiktionary