补充：其实类似的能源物质不止于S、H₂S、H₂和CH₄，海底一种嗜酸嗜热古菌Acidianus A1-3体内的二硫化碳水解酶能够将CS₂转变成H₂S和CO₂，为自身的生命活动提供能量。详见

Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon

• Marjan J. Smeulders^{1, 5} Thomas R. M. Barends^{2, 5} Arjan Pol¹ Anna Scherer² Marcel H. Zandvoort¹ Anikó Udvarhelyi² Ahmad F. Khadem¹ Andreas Menzel³ John Hermans¹ Robert L. Shoeman² Hans J. C. T. Wessels⁴ Lambert P. van den Heuvel⁴ Lina Russ¹ Ilme Schlichting² Mike S. M. Jetten¹ Huub J. M. Op den Camp¹ Affiliations Contributions Corresponding author 

Journal name: Nature Volume: 478, Pages:412–416 DOI: doi:10.1038/nature10464

Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide (H₂S) and carbon disulphide (CS₂)^{1, 2}. The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert CS₂ into H₂S and carbon dioxide (CO₂), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a CS₂ hydrolase from Acidianus A1-3. The enzyme monomer displays a typical β-carbonic anhydrase fold and active site, yet CO₂ is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical β-carbonic anhydrases and the formation of a single 15-Å-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme’s substrate specificity for CS₂, which is hydrophobic. The transposon sequences that surround the gene encoding this CS₂ hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient β-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in CS₂ metabolism.