In a previous publication (2) a double displacement mechanism for the catalytic activity of rhodanese (thiosulfate cyanide sulfurtransferase) was proposed on the basis of polarographic evidence. In addition it was concluded from the polarographic data that crystahine beef liver rhodanese is an enzyme-substrate intermediate containing two activated substrate sulfur atoms per molecule. This commu...

Rhodanese domains are ubiquitous structural modules occurring in the three major evolutionary phyla. They are found as tandem repeats, with the C-terminal domain hosting the properly structured active-site Cys residue, as single domain proteins or in combination with distinct protein domains. An increasing number of reports indicate that rhodanese modules are versatile sulfur carriers that have...

The activities of the enzymes arginase and rhodanese were examined in homogenates of 13 mouse cell strains and 2 human cell strains after long cultivation of the cells in vitro. Three strains of mouse liver origin showed both high arginase and rhodanese activities in keeping with activities of the tissue of origin. Two strains of cells of human epithelial origin, HeLa and epidermis, were found ...

Present studies have focused on a novel cyanide antidotal system, on the coencapsulation of a new sulfur donor DTO with rhodanese within sterically stabilized liposomes. The optimal lipid composition for coencapsulation of DTO with rhodanese is the combination of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, cholesterol, cationic lipid (DOTAP), and 1,2-dipalmitoyl-sn-glycero-3-phosphoethano...

In the course of the reaction catalyzed by rhodanese, the enzyme cycles between two catalytic intermediates, the sulfur-free and the sulfur-substituted (persulfide-containing) forms. The crystal structure of sulfur-free rhodanese, which was prepared in solution and then crystallized, is highly similar to that of sulfur-substituted enzyme. The inactivation of sulfur-free rhodanese with a small m...

The GroEL/GroES chaperonin system acts as a passive anti-aggregation cage for refolding rubisco and rhodanese, and not as an active unfolding device. Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese.

Controlled conditions have been found that give complete reactivation and long term stabilization of rhodanese (EC 2.8.1.1) after oxidative inactivation by hydrogen peroxide. Inactivated rhodanese was completely reactivated by reductants such as thioglycolic acid (TGA) (100 mM) and dithiothreitol (DTT) (100 mM) or the substrate thiosulfate (100 mM) if these reagents were added soon after inacti...

A molecular dynamics simulation of the active unfolding of denatured rhodanese by the chaperone GroEL is presented. The compact denatured protein is bound initially to the cis cavity and forms stable contacts with several of the subunits. As the cis ring apical domains of GroEL undergo the transition from the closed to the more open (ATP-bound) state, they exert a force on rhodanese that leads ...

The purpose of this investigation was to determine and compare the activities of arginase and rhodanese in the blood plasma of cigarette smokers and non-smokers.The activity of arginase in the blood plasma of smokers was higher than arginase activity in the non-smokers (NS), however,in the smokers with diseases (SWD), the increase was significant. The comparison between the activity of rhodanes...