Magnetic behavior of a mixed Ising 3/2 and 5/2 spin model.

We perform Monte Carlo simulations in order to study the magnetic properties of the mixed spin-S = ± 3/2, ± 1/2 and spin-σ = ± 5/2, ± 3/2, ± 1/2 Ising model. The spins are alternated on a square lattice such that S and σ are nearest neighbors. We found that when the Hamiltonian includes antiferromagnetic interactions between the S and σ spins, ferromagnetic interactions between the spins S, and a crystal field, the system presents compensation temperatures in a certain range of the parameters. The compensation temperatures are temperatures below the critical point where the total magnetization is zero, and they have important technological applications. We calculate the finite-temperature phase diagrams of the system. We found that the existence of compensation temperatures depends on the strength of the ferromagnetic interaction between the S spins.

Nitric oxide interaction with cytochrome c' and its relevance to guanylate cyclase. Why does the iron histidine bond break?

Soluble guanylate cyclase (sGC), the mammalian receptor for nitric oxide (NO), is a heme protein with a histidine as the proximal ligand. Formation of a five-coordinate heme-NO complex with the associated Fe-His bond cleavage is believed to trigger a conformational change that activates the enzyme and transduces the NO signal. Cytochrome c' (cyt c') is a protobacteria heme protein that has several similarities with sGC, including the ability to form a five-coordinate NO adduct and the fact that it does not bind oxygen. Recent crystallographic characterization of cyt c' from Alcaligenes xylosoxidans (AXCP) has yielded the discovery that exogenous ligands are able to bind to the Fe center from either side of the porphyrin plane. In this paper, we explore the molecular basis of the NO interaction with AXCP using hybrid quantum-classical simulation techniques. Our results suggest that Fe-His bond breaking depends not only on the iron-histidine bond strength but also on the existence of a local minimum conformation of the protein with the histidine away from the iron. We also show that AXCP is a useful paradigm for NO interaction with heme proteins, particularly regarding the activation/deactivation mechanism of sGC. The results presented here fully support a recently proposed model of sGC activation in which NO is not only the iron ligand but also catalyzes the activation step.