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
N1 - Funding Information:
We thank the North Carolina Supercomputing Center for a generous grant of time on the Cray T90 system. LGP appreciates support from NIH for grant HL-06350 and the opportunity to work at NIEHS, RTP over a number of summers. LGP dedicates this paper to KM on the event of his 65th birthday and with good memories of 1965–1967 in the Karplus group at Columbia and Harvard.
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 -