The binding of sulfate, selenate and thiosulfate by the sulfur-transferase rhodanese (EC 2.8.1.1) in the crystalline state has been studied by X-ray analysis at resolutions between 0.23 nm and 0.4 nm. The three ions appear to occupy a common site between the N V atoms of Arg-29 and the main-chain NH group of Glu-148 at the surface of the enzyme molecule.A second binding site for the three ions is situated at the entrance to the active centre, between the side chains of Arg-186 and Lys-249. Selenate and thiosulfate are bound equally well at both anion-binding sites. Sulfate, however, binds better at the first position, near Arg-29. than at the second site near Arg-186.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 Sy of the essential Cys-247. The distance between the outer sulfur atom of the thiosulfate ion and the persulfide sulfur atom appears to be about 0.3 nm.The thiosulfate difference Fourier also shows a distinct, localized conformational change involving residues 71, 72 and 249. This is the result of the replacement of an ammonium ion in the sulfate and selenate media by a sodium ion in the sodium thiosulfate solution. Rhodanese is apparently able to accomodate ions with different radii at this cation-binding site by minor structural alterations.Rhodanese, or thiosulfate sulfurtransferase, is an enzyme which occurs in many organisms. This suggests that it has an important biological function. However, despite a large number of investigations, the major function or functions of rhodanese have not yet becn unequivocally established. Originally it was thought that rhodanese was only involved in countering cyanide intoxication, which may arise in the mammalian metabolism, in particular from the consumption of plant material containing cyanogenic glycosides [l], but other possible functions have since been proposed. A recent report suggested even a link of rhodanese deficiency in human liver with Leber's optic atrophy [2]. At the molecular level indications have been found that rhodanese might be a 'sulfur insertase' and play a role in the construction or repair of Fe-S clusters in proteins like ferredoxin [3], succinate dehydrogenase [4] and NADH dehydrogenase [5]. Westley, on the other hand, has emphasized the possible role of rhodanese in maintaining the sulfane sulfur pool in living organisms [6,7]. It may therefore well be that rhodanese is a multi-functional enzyme with, perhaps, different functions being utilized in different organisms or organs.Although rhodanese has been found in a wide variety of organisms [1,8], most research has been done on the enzyme Abbrmiations. Rhod-S, rhodanese with a sulfur atom bound to the S of Cys-247 ; MIRAS, multiple isomorphous replacement method including anomalous scattering; lFObFl, l~.,,cl ; observed and calculated structure factor amplitudes, respectively.Enzyme. Rhodanese or thiosu1fate:cyanide sulfurtransferase (EC 2.8.1.1). ...
An interactive graphics program is described for use with the Evans & Sutherland Picture System 2 which is suitable for the comparison and refinement of protein structures. Several protein molecules and electron density maps can be viewed simultaneously, while great flexibility exists in creating, modifying and manipulating the picture on the screen. As the program is file oriented, it can be run on a small computer system with only 32 K memory.
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. (1978) Arch. Biochem. Biophys. 191, 205-215]. Crystallographic studies are described which reveal the binding mode of four different metal cyanides to bovine liver rhodanese: Na[Au(CN2], K2[Pt(CN)4], K2[Ni(CN)4], and K2[Zn(CN)4]. It appears that these complexes bind at one common site at the entrance of the active site pocket, interacting with the positively charged side chains of Arg-186 and Lys-249. This observation explains the inhibition of rhodanese by this class of compounds. For the platinum and nickel cyanide complexes virtually no other binding sites are observed. 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. The zinc complex binds to completely different additional sites and forms complexes with the side chains of Asp-101 and His-203. Possible reasons for these different binding modes are discussed in terms of the preference for "hard" and "soft" ligands of these four metal ions.
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