Thiosulfate-Cyanide Sulfurtransferase a Mitochondrial Essential Enzyme: From Cell Metabolism to the Biotechnological Applications

Abstract

Thiosulfate: cyanide sulfurtransferase (TST), also named rhodanese, is an enzyme widely distributed in both prokaryotes and eukaryotes, where it plays a relevant role in mitochondrial function. TST enzyme is involved in several biochemical processes such as: cyanide detoxification, the transport of sulfur and selenium in biologically available forms, the restoration of iron-sulfur clusters, redox system maintenance and the mitochondrial import of 5S rRNA. Recently, the relevance of TST in metabolic diseases, such as diabetes, has been highlighted, opening the way for research on important aspects of sulfur metabolism in diabetes. This review underlines the structural and functional characteristics of TST, describing the physiological role and biomedical and biotechnological applications of this essential enzyme.

Keywords: alpha-beta domain; biotechnology; cyanide; hydrogen sulfide; iron-sulfur clusters; redox system; rhodanese.

Figure 1

Scheme of the ping-pong mechanism of the sulfur transfer reaction catalyzed by TST/rhodanese.

Figure 2

Cartoon representation of 3D structures of thiosulfate: cyanide sulfurtransferases with tandem and single domain. (https://www.rcsb.org/) TSTbov (1 orb) [45], TSTD1 (6 bev) [33], GLlpE (1 gmx) [21] and PspE (2 jtq) [58].

Figure 3

Schematic representation of the functional roles of TST: in cyanide detoxification by thiocyanate formation; in the respiratory complex by Fe-S-cluster formation; in the redox system by thioredoxin and glutathione restoration and hydrogen sulfide oxidation.

Figure 4

Schematic description of the diseases where TST expression and activity were suggested to play a relevant role.