• Publications
  • Influence
Structural aspects of metal liganding to functional groups in proteins.
  • J. Glusker
  • Chemistry, Medicine
  • Advances in protein chemistry
  • 1991
The properties of metals that are useful in the structure and function of proteins, particularly enzymes, and the geometry of interaction of metals with the various chemical groups of proteins are emphasized and the stereochemistry of liganding of metal ions in proteins is emphasized. Expand
Calcium Ion Coordination: A Comparison with That of Beryllium, Magnesium, and Zinc
The coordination geometry of divalent calcium ions has been investigated by analyses of the crystal structures of small molecules containing this cation that are found in the Cambridge StructuralExpand
Manganese as a Replacement for Magnesium and Zinc: Functional Comparison of the Divalent Ions
Divalent manganese, magnesium, and zinc fill unique roles in biological systems, despite many apparently similar chemical properties. A comparison of the liganding properties of divalent manganese,Expand
Reactivity and inhibitor potential of hydroxycitrate isomers with citrate synthase, citrate lyase, and ATP citrate lyase.
It is proposed that more than one mode of binding is possible between the isomers and the three different active sites of hydroxycitrate. Expand
Crystal Structure Analysis for Chemists and Biologists
Introduction to Crystal Structure Analysis. Crystals. Diffraction by Crystals. Symmetry in Crystals and their Diffraction Patterns. Physical Properties of Crystals. Combining Waves to Obtain anExpand
Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study.
The structure of the metalloenzyme D-xylose isomerase is determined by neutron diffraction in order to locate H atoms (or their isotope D) and the results lead to new suggestions as to how changes might take place over the course of the reaction. Expand
Hydrogen location in stages of an enzyme-catalyzed reaction: time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose.
The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme d-xylose isomerase (XI). The neutron structure of crystalline XI with bound product,Expand
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction.
Time-of-flight neutron diffraction has been used to locate hydrogen atoms that define the ionization states of amino acids in crystals of D-xylose isomerase, and the position and orientation of a metal ion-bound water molecule that is located in the active site of the enzyme is determined. Expand
X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator.
The changes in structure of the native enzyme, the enzyme with bound substrate, and the alkylated enzyme indicate that the mechanism involves an "open-chain" conformation of substrate and that the intermediate in the isomerization reaction is probably a cis-ene diol because the active-site histidine is correctly placed to abstract a proton from C1 or C2 of the substrate. Expand
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase.
Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show that there are a variety of binding modes and possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated. Expand