Abstract
The biological process of enzymatic sulfuryl group transfer has been studied by ab initio (density-functional and Hartree-Fock) and semiempirical quantum mechanical methods. The active site of estrogen sulfotransferase in ternary complex with a sulfate donor (PAPS) and sulfate acceptor (estradiol) is modeled. The mechanism proposed in a recent X-ray crystal structure paper (Kakuta et al., Nat. Struct. Biol. 4 (1997) 904) serves as the basis for the calculations. We find that the mechanism proposed in the crystallographic paper is reasonable. The sulfonation takes place in several key steps: neutralization of the charge on PAPS, lengthening of the bridging S-O bond with no cost in energy, activation of the attacking oxygen and proton transfer from estradiol to histidine and then to the sulfuryl group.
| Original language | English |
|---|---|
| Pages (from-to) | 105-111 |
| Number of pages | 7 |
| Journal | Journal of Molecular Structure: THEOCHEM |
| Volume | 461-462 |
| DOIs | |
| Publication status | Published - Apr 2 1999 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Condensed Matter Physics
- Physical and Theoretical Chemistry
Cite this
A quantum mechanical study of the transfer of biological sulfate. / Bartolotti, Lee; Kakuta, Yoshimitsu; Pedersen, Lars; Negishi, Masahiko; Pedersen, Lee.
In: Journal of Molecular Structure: THEOCHEM, Vol. 461-462, 02.04.1999, p. 105-111.Research output: Contribution to journal › Article
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TY - JOUR
T1 - A quantum mechanical study of the transfer of biological sulfate
AU - Bartolotti, Lee
AU - Kakuta, Yoshimitsu
AU - Pedersen, Lars
AU - Negishi, Masahiko
AU - Pedersen, Lee
PY - 1999/4/2
Y1 - 1999/4/2
N2 - The biological process of enzymatic sulfuryl group transfer has been studied by ab initio (density-functional and Hartree-Fock) and semiempirical quantum mechanical methods. The active site of estrogen sulfotransferase in ternary complex with a sulfate donor (PAPS) and sulfate acceptor (estradiol) is modeled. The mechanism proposed in a recent X-ray crystal structure paper (Kakuta et al., Nat. Struct. Biol. 4 (1997) 904) serves as the basis for the calculations. We find that the mechanism proposed in the crystallographic paper is reasonable. The sulfonation takes place in several key steps: neutralization of the charge on PAPS, lengthening of the bridging S-O bond with no cost in energy, activation of the attacking oxygen and proton transfer from estradiol to histidine and then to the sulfuryl group.
AB - The biological process of enzymatic sulfuryl group transfer has been studied by ab initio (density-functional and Hartree-Fock) and semiempirical quantum mechanical methods. The active site of estrogen sulfotransferase in ternary complex with a sulfate donor (PAPS) and sulfate acceptor (estradiol) is modeled. The mechanism proposed in a recent X-ray crystal structure paper (Kakuta et al., Nat. Struct. Biol. 4 (1997) 904) serves as the basis for the calculations. We find that the mechanism proposed in the crystallographic paper is reasonable. The sulfonation takes place in several key steps: neutralization of the charge on PAPS, lengthening of the bridging S-O bond with no cost in energy, activation of the attacking oxygen and proton transfer from estradiol to histidine and then to the sulfuryl group.
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U2 - 10.1016/S0166-1280(98)00424-2
DO - 10.1016/S0166-1280(98)00424-2
M3 - Article
AN - SCOPUS:0033515372
VL - 461-462
SP - 105
EP - 111
JO - Computational and Theoretical Chemistry
JF - Computational and Theoretical Chemistry
SN - 2210-271X
ER -