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- W2091582792 abstract "Detailed theoretical and X-ray based structural analysis has been carried out in order to unmask the role of the tyrosine residue (Y) in the activation of the Co−C bond in AdoCbl-dependent mutases. In particular, methylmalonyl-CoA mutase (MCM) and glutamate mutase (GLM) enzymes have been studied; in the case of MCM, the significance of the Y89 residue has been analyzed extensively. Three different theoretical platforms encompassing the DFT, CASSCF/QDPT2, and QM/MM frameworks have been employed to elucidate the energetics of the AdoCbl−Y− complex while taking into account a varied degree of structural complexity. The diradical state, [AdoCbl]•−−Y•, has been found to be the lowest electronic state of the AdoCbl−Y− complex, providing strong evidence that electron transfer from the Y89 residue to the cofactor is feasible. Crystallographic analysis of the active sites of MCM and GLM enzymes reveals that substrate binding can play a critical role in displacing the hydroxyl proton of the Y residue (Y89 in the case of MCM enzyme and Y181 in the case of GLM enzyme) that will facilitate the electron transfer (ET), hence making the activation process a case of proton-coupled electron transfer (PCET). PCET-inspired enzymatic catalysis implies that the cleavage of the Co−C bond takes place via one-electron reduced form of the AdoCbl cofactor (i.e., [AdoCbl]•−), rather than its neutral analogue, thus providing an efficient mode of cleavage that can help in understanding the origin of the catalytic effect in such enzymes." @default.
- W2091582792 created "2016-06-24" @default.
- W2091582792 creator A5008539128 @default.
- W2091582792 creator A5038453378 @default.
- W2091582792 creator A5046071586 @default.
- W2091582792 creator A5065640728 @default.
- W2091582792 creator A5078131690 @default.
- W2091582792 date "2010-04-13" @default.
- W2091582792 modified "2023-09-23" @default.
- W2091582792 title "Theoretical Analysis of the Diradical Nature of Adenosylcobalamin Cofactor−Tyrosine Complex in B<sub>12</sub>-Dependent Mutases: Inspiring PCET-Driven Enzymatic Catalysis" @default.
- W2091582792 cites W1500324843 @default.
- W2091582792 cites W1503569245 @default.
- W2091582792 cites W1508531955 @default.
- W2091582792 cites W1553119709 @default.
- W2091582792 cites W1556997704 @default.
- W2091582792 cites W1636387388 @default.
- W2091582792 cites W1640573482 @default.
- W2091582792 cites W1963683620 @default.
- W2091582792 cites W1965546470 @default.
- W2091582792 cites W1965788129 @default.
- W2091582792 cites W1972040015 @default.
- W2091582792 cites W1972400761 @default.
- W2091582792 cites W1974471377 @default.
- W2091582792 cites W1978146620 @default.
- W2091582792 cites W1978871721 @default.
- W2091582792 cites W1979035606 @default.
- W2091582792 cites W1980675359 @default.
- W2091582792 cites W1981731218 @default.
- W2091582792 cites W1983311793 @default.
- W2091582792 cites W1988099644 @default.
- W2091582792 cites W1989282758 @default.
- W2091582792 cites W1991692701 @default.
- W2091582792 cites W1993072233 @default.
- W2091582792 cites W1993178021 @default.
- W2091582792 cites W1995089314 @default.
- W2091582792 cites W1996408951 @default.
- W2091582792 cites W1997160871 @default.
- W2091582792 cites W1998891503 @default.
- W2091582792 cites W2002551641 @default.
- W2091582792 cites W2006610149 @default.
- W2091582792 cites W2011551228 @default.
- W2091582792 cites W2012678539 @default.
- W2091582792 cites W2021744522 @default.
- W2091582792 cites W2021745376 @default.
- W2091582792 cites W2022046410 @default.
- W2091582792 cites W2023625778 @default.
- W2091582792 cites W2024603528 @default.
- W2091582792 cites W2024737166 @default.
- W2091582792 cites W2025683108 @default.
- W2091582792 cites W2026961999 @default.
- W2091582792 cites W2028022118 @default.
- W2091582792 cites W2030234420 @default.
- W2091582792 cites W2030687437 @default.
- W2091582792 cites W2031745865 @default.
- W2091582792 cites W2032839609 @default.
- W2091582792 cites W2034294731 @default.
- W2091582792 cites W2040891489 @default.
- W2091582792 cites W2042839694 @default.
- W2091582792 cites W2047413915 @default.
- W2091582792 cites W2048036692 @default.
- W2091582792 cites W2050350740 @default.
- W2091582792 cites W2052315960 @default.
- W2091582792 cites W2053731321 @default.
- W2091582792 cites W2055330686 @default.
- W2091582792 cites W2056768042 @default.
- W2091582792 cites W2056967289 @default.
- W2091582792 cites W2057571164 @default.
- W2091582792 cites W2060408358 @default.
- W2091582792 cites W2060645914 @default.
- W2091582792 cites W2063783087 @default.
- W2091582792 cites W2070797882 @default.
- W2091582792 cites W2072447108 @default.
- W2091582792 cites W2074824070 @default.
- W2091582792 cites W2076605403 @default.
- W2091582792 cites W2077392737 @default.
- W2091582792 cites W2077466875 @default.
- W2091582792 cites W2078289393 @default.
- W2091582792 cites W2078935376 @default.
- W2091582792 cites W2079108392 @default.
- W2091582792 cites W2083453646 @default.
- W2091582792 cites W2084548015 @default.
- W2091582792 cites W2084851321 @default.
- W2091582792 cites W2084911457 @default.
- W2091582792 cites W2087406097 @default.
- W2091582792 cites W2092324522 @default.
- W2091582792 cites W2094537108 @default.
- W2091582792 cites W2094930728 @default.
- W2091582792 cites W2095259787 @default.
- W2091582792 cites W2106005716 @default.
- W2091582792 cites W2111413667 @default.
- W2091582792 cites W2112356473 @default.
- W2091582792 cites W2114974455 @default.
- W2091582792 cites W2120474267 @default.
- W2091582792 cites W2121243460 @default.
- W2091582792 cites W2131508970 @default.
- W2091582792 cites W2137460896 @default.
- W2091582792 cites W2138461375 @default.
- W2091582792 cites W2146440582 @default.