Molecular Orbital Study of the Interaction between MgATP and the Myosin Motor Domain: The Highest Occupied Molecular Orbitals Indicate the Reaction Site of ATP Hydrolysis
- 1 August 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 103 (34) , 7346-7352
- https://doi.org/10.1021/jp991117g
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Actomyosin interaction in striated musclePhysiological Reviews, 1997
- Active site comparisons highlight structural similarities between myosin and other P-loop proteinsBiophysical Journal, 1996
- X-ray Structures of the Myosin Motor Domain of Dictyostelium discoideum Complexed with MgADP.cntdot.BeFx and MgADP.cntdot.AlF4-Biochemistry, 1995
- GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4Nature, 1994
- Optimization of parameters for semiempirical methods. III Extension of PM3 to Be, Mg, Zn, Ga, Ge, As, Se, Cd, In, Sn, Sb, Te, Hg, Tl, Pb, and BiJournal of Computational Chemistry, 1991
- Optimization of parameters for semiempirical methods II. ApplicationsJournal of Computational Chemistry, 1989
- Why is Mg2+ necessary for specific cleavage of the terminal phosphoryl group of ATP?Biophysical Chemistry, 1987
- A Molecular Orbital Treatment of Phosphate Bonds of Biochemical Interest. II. Metal Chelates of Adenosine TriphosphateBulletin of the Chemical Society of Japan, 1963
- A Molecular Orbital Treatment of Phosphate Bonds of Biochemical Interest. I. Simple LCAO MO TreatmentBulletin of the Chemical Society of Japan, 1960
- Molecular Orbital Theory of Orientation in Aromatic, Heteroaromatic, and Other Conjugated MoleculesThe Journal of Chemical Physics, 1954