PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10788330-1 2000 Rhodanese is an ubiquitous enzyme that in vitro catalyses the transfer of a sulfur atom from suitable donors to nucleophilic acceptors by way of a double displacement mechanism. Sulfur 76-82 thiosulfate sulfurtransferase Bos taurus 0-9 10788330-4 2000 The crystal structure of the A. vinelandii rhodanese has been determined and refined at 1.8 A resolution in the sulfur-free and persulfide-containing forms. Sulfur 112-118 thiosulfate sulfurtransferase Bos taurus 43-52 2492522-8 1989 The phosphorylation site is accessible in rhodanese that is free of substrate sulfur but not in the covalent enzyme-sulfur intermediate which is formed as an obligatory step during the course of catalysis. Sulfur 78-84 thiosulfate sulfurtransferase Bos taurus 42-51 1667623-0 1991 Improved method for measurement of rhodanese activity using methanethiosulfonate as sulfur donor substrate and its application to human serum. Sulfur 84-90 thiosulfate sulfurtransferase Bos taurus 35-44 2317511-8 1990 Sulfane sulfurtransferase, like rhodanese, catalyzes the transfer of sulfur from thiosulfate to cyanide via a persulfide intermediate, and displays remarkably similar kinetics in this process (Aird, B.A., Heinrikson, R.L. Sulfur 8-14 thiosulfate sulfurtransferase Bos taurus 32-41 2317511-12 1990 In light of this, the results of the structural studies with sulfane sulfurtransferase are compared and contrasted to data from similar experiments with rhodanese in hopes that they would provide insight about which phenomena observed with rhodanese are intrinsic to the process of transferring sulfur atoms. Sulfur 69-75 thiosulfate sulfurtransferase Bos taurus 240-249 2492522-13 1989 Rhodanese, in turn, serves as a converter enzyme which directly alters the rate of the respiratory chain and, thus, ATP production by the reversible sulfuration of key iron-sulfur centers. Sulfur 149-155 thiosulfate sulfurtransferase Bos taurus 0-9 6575830-1 1983 Bovine liver rhodanese, which catalyzes the transfer of sulfur atoms between a variety of sulfur donor and sulfur acceptor substrates, is inhibited by metal cyanide complexes [Volini, M., Van Sweringen, B., & Chen, F.-Sh. Sulfur 56-62 thiosulfate sulfurtransferase Bos taurus 13-22 3460592-1 1986 Mitochondrial bovine liver rhodanese (thiosulfate:cyanide sulfurtransferase) has been crystallized in the form deprived of the transferable sulfur. Sulfur 58-64 thiosulfate sulfurtransferase Bos taurus 27-36 2992467-2 1985 Rhodanese, also a mitochondrial enzyme, is thought to be required for synthesis of iron-sulfur centers, such as those contained in adrenodoxin. Sulfur 88-94 thiosulfate sulfurtransferase Bos taurus 0-9 6357922-1 1983 The crystal structure of the sulfur complex of bovine liver rhodanese has been determined at a resolution of 2.1 A. Sulfur 29-35 thiosulfate sulfurtransferase Bos taurus 60-69 3466649-0 1987 Chemical modification of bovine liver rhodanese with tetrathionate: differential effects on the sulfur-free and sulfur-containing catalytic intermediates. Sulfur 96-102 thiosulfate sulfurtransferase Bos taurus 38-47 3466649-0 1987 Chemical modification of bovine liver rhodanese with tetrathionate: differential effects on the sulfur-free and sulfur-containing catalytic intermediates. Sulfur 112-118 thiosulfate sulfurtransferase Bos taurus 38-47 3466649-3 1987 At a ratio of one tetrathionate per mole of rhodanese, 100% of enzyme activity was lost in the sulfur-free E-form as compared with a 70% loss for the sulfur-containing ES-form of the enzyme. Sulfur 95-101 thiosulfate sulfurtransferase Bos taurus 44-53 3466649-3 1987 At a ratio of one tetrathionate per mole of rhodanese, 100% of enzyme activity was lost in the sulfur-free E-form as compared with a 70% loss for the sulfur-containing ES-form of the enzyme. Sulfur 150-156 thiosulfate sulfurtransferase Bos taurus 44-53 6589161-7 1984 In the complex of sulfur-rhodanese with thiosulfate, the outer sulfur atom of the anion near the active centre points towards the extra sulfur atom which is bound as a persulfide to the S gamma of the essential Cys-247. Sulfur 18-24 thiosulfate sulfurtransferase Bos taurus 25-34 6589161-7 1984 In the complex of sulfur-rhodanese with thiosulfate, the outer sulfur atom of the anion near the active centre points towards the extra sulfur atom which is bound as a persulfide to the S gamma of the essential Cys-247. Sulfur 63-69 thiosulfate sulfurtransferase Bos taurus 25-34 6575830-1 1983 Bovine liver rhodanese, which catalyzes the transfer of sulfur atoms between a variety of sulfur donor and sulfur acceptor substrates, is inhibited by metal cyanide complexes [Volini, M., Van Sweringen, B., & Chen, F.-Sh. Sulfur 90-96 thiosulfate sulfurtransferase Bos taurus 13-22 6575830-1 1983 Bovine liver rhodanese, which catalyzes the transfer of sulfur atoms between a variety of sulfur donor and sulfur acceptor substrates, is inhibited by metal cyanide complexes [Volini, M., Van Sweringen, B., & Chen, F.-Sh. Sulfur 90-96 thiosulfate sulfurtransferase Bos taurus 13-22 6575830-10 1983 The gold complex binds, however, to three additional cysteine residues, thereby also displacing the extra sulfur atom which was bound to the essential Cys-247 in the sulfur-rhodanese complex. Sulfur 106-112 thiosulfate sulfurtransferase Bos taurus 173-182 986188-2 1976 This reagent, in the absence of thiosulfate, reduces the amount of sulfur carried by rhodanese with formation of sulfide and oxidized dithiothreitol: E-S-SH + reduced dithiothreitol replaced by E-SH + HS- + oxidized dithiothreitol, (E = enzyme). Sulfur 67-73 thiosulfate sulfurtransferase Bos taurus 85-94 6402020-6 1983 Rhodanese-mediated sulfide transfer was directly demonstrated when the reactivation of NADH dehydrogenase was performed in the presence of radioactive thiosulfate (labeled in the outer sulfur) and the 35S-loaded flavoprotein was re-isolated by gel filtration chromatography. Sulfur 185-191 thiosulfate sulfurtransferase Bos taurus 0-9 711738-2 1978 Chemical modification studies of bovine liver rhodanese have underscored important distinctions between free rhodanese and the catalytic intermediate in which the sulfane atom of the sulfur donor is bound covalently to the enzyme (sulfur-rhodanese). Sulfur 183-189 thiosulfate sulfurtransferase Bos taurus 46-55 711738-2 1978 Chemical modification studies of bovine liver rhodanese have underscored important distinctions between free rhodanese and the catalytic intermediate in which the sulfane atom of the sulfur donor is bound covalently to the enzyme (sulfur-rhodanese). Sulfur 183-189 thiosulfate sulfurtransferase Bos taurus 109-118 711738-2 1978 Chemical modification studies of bovine liver rhodanese have underscored important distinctions between free rhodanese and the catalytic intermediate in which the sulfane atom of the sulfur donor is bound covalently to the enzyme (sulfur-rhodanese). Sulfur 183-189 thiosulfate sulfurtransferase Bos taurus 109-118 711738-4 1978 Analysis of rate data for the iodoacetate reaction showed that the apparent pK of this group is 7.8 in free rhodanese and 6.7 to 7.0 in complexes of the enzyme with analogs of sulfur donor substrates, in agreement with the previous inference from steady state kinetic observations. Sulfur 176-182 thiosulfate sulfurtransferase Bos taurus 108-117 711738-6 1978 In contrast to these results with free rhodanese, the sulfur-substituted enzyme is not inactivated by iodoacetate and is only relatively slowly inactivted by treatment with substantial excesses of phenylglyoxal. Sulfur 54-60 thiosulfate sulfurtransferase Bos taurus 39-48 20135153-2 2011 The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate. Sulfur 111-117 thiosulfate sulfurtransferase Bos taurus 37-46