Quantum Catalysis Research Articles

Partial recovery of quantum entanglement

Suppose Alice and Bob try to transform an entangled state shared between them into another one by local operations and classical communications. Then in general a certain amount of entanglement contained in the initial state will decrease in the process of transformation. However, an interesting phenomenon called partial entanglement recovery shows that it is possible to recover some amount of entanglement by adding another entangled state and transforming the two entangled states collectively. In this paper, we are mainly concerned with the feasibility of partial entanglement recovery. The basic problem we address is whether a given state is useful in recovering entanglement lost in a specified transformation. In the case where the source and target states of the original transformation satisfy the strict majorization relation, a necessary and sufficient condition for partial entanglement recovery is obtained. For the general case we give two sufficient conditions. We also give an efficient algorithm for the feasibility of partial entanglement recovery in polynomial time. As applications, we establish some interesting connections between partial entanglement recovery and the generation of maximally entangled states, quantum catalysis, mutual catalysis, and multiple-copy entanglement transformation.

Quantum catalysis in enzymes: beyond the transition state theory paradigm. A Discussion Meeting held at the Royal Society on 14 and 15 November 2005

How do enzymes work? What is the physical basis of the phenomenal rate enhancements achieved by enzymes? Do we have a theoretical framework that accounts for observed catalytic rates? These are the foremost questions-with particular emphasis on tunnelling phenomena-debated at this Discussion Meeting by the leading practitioners in the field.

Quantum Catalysis [Conferences & Workshops

Quantum Catalysis [Conferences & Workshops

Quantum chemistry and catalysis

Why do platinum, palladium, nickel and iron, as well as other Group-VIII transition metals, continually turn up as the active sites in catalysts? Why do certain enzymes and proteins—substances such as hemoglobin and ferredoxin that catalyze metabolic processes in living organisms—also appear to rely on transition metals for their action? How do catalysts work anyway, and could we design better ones? We are much nearer answering these questions and other related ones now that new methods, both theoretical and experimental, are available to investigate the electronic structure of complex molecules and materials of the type important to catalysis.