Preface 1. Introduction 2. Haemoglobin: Dependence of allosteric equilibrium on spin state and coordination of the haem iron 3. Haemocyanin: Dependence of allosteric equilibrium on coordination and valency of a binuclear copper complex 4. Haemerythrin: Cooperativity in a binuclear iron complex 5. Glycogen phosphorylase: Control of glycolysis 6. Phosphofructokinase: Further control of glycolysis 7. Feedback inhibition of a biosynthetic pathway: Aspartate Transcarbamoylase 8. Control of nitrogen metabolism: Glutamine synthetase 9. Cooperativity and feedback inhibition without change of quaternary structure: The "trp" and "met" repressors of E. Coli 10. Immunoglobulins: Cooperative binding to multivalent antigens 11. Allosteric membrane proteins.

Mechanisms of Cooperativity and Allosteric Regulation in Proteins

Many metalloenzymes exhibit distinctive spectral features that are now becoming well understood. These reflect active site electronic structures that can make significant contributions to catalysis. Copper proteins provide well-characterized examples in which the unusual electronic structures of their active sites contribute to rapid, long-range electron transfer reactivity, oxygen binding and activation, and the multielectron reduction of dioxygen to water.

https://science.sciencemag.org/content/sci/259/5101/1575.full.pdf

Electronic structure contributions to function in bioinorganic chemistry

The activation of small molecules by dinuclear complexes of copper and other metals

XAFS, IR, and UV−vis (diffuse reflectance and photoluminescence) spectroscopies have been employed to investigate the local environment of CuI in CuI-ZSM-5 prepared by gas phase reaction of H-ZSM-5 (SiO2/Al2O3 = 90−50) with CuCl The measurements confirm that the absolutely predominant copper species formed with this procedure are CuI:Cu species in other oxidation states are less than 1% Direct proof of the absence of both unreacted CuCl microaggregates and of copper clusters in the zeolite channels is also given CuI-ZSM-5 prepared in this way represents a model solid for investigating the structure of isolated CuI sites in zeolites EXAFS analysis reveal that, in vacuum conditions, Cu+ cations are surrounded by 25 ± 03 oxygens at 200 ± 002 A The combined use of EXAFS, IR, and photoluminescence UV−vis spectroscopies and computer graphic simulations allows to infer that Cu+ ions in CuI-ZSM-5 are located in two families of sites, indicated as I and II, (site II having the highest coordinative unsatur

XAFS, IR, and UV−Vis Study of the CuI Environment in CuI-ZSM-5

For the first time, the three-dimensional structure of a member of the copper-containing class of oxygen-carrying proteins—the haemocyanins—has been determined. The structure of Panulirus interruptus haemocyanin at 3.2 A resolution shows that each subunit of the 450,000-molecular weight hexamer is folded into three domains, and that the binuclear copper site is situated in the centre of the second domain. Amino acid sequence comparisons suggest that the polypeptide fold of P. interruptus haemocyanin is common to all arthropod haemocyanins.

J. M. Brown

Papers

Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis

Structural studies of the hemocyanin active site. 1. extended x-ray absorption fine structure (exafs) analysis

Hemocyanin Active Site Characterization by EXAFS and Resonance Raman Spectroscopy