Natural history and the formation of the human being: Kant on active forces

In his 1785-review of the Ideen zur Philosophie der Geschichte der Menschheit, Kant objects to Herder's conception of nature as being imbued with active forces. This attack is usually evaluated against the background of Kant's critical project and his epistemological concern to caution against the “metaphysical excess” of attributing immanent properties to matter. In this paper I explore a slightly different reading by investigating Kant's pre-critical account of creation and generation. The aim of this is to show that Kant's struggle with the forces of matter has a long history and revolves around one central problem: that of how to distinguish between the non-purposive forces of nature and the intentional powers of the mind. Given this history, the epistemic stricture that Kant's critical project imposes on him no longer appears to be the primary reason for his attack on Herder. It merely aggravates a problem that Kant has been battling with since his earliest writings.     

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

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 (H(2)S) and carbon disulphide (CS(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 CS(2) into H(2)S and carbon dioxide (CO(2)), 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 CS(2) hydrolase from Acidianus A1-3. The enzyme monomer displays a typical β-carbonic anhydrase fold and active site, yet CO(2) 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-?-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for CS(2), which is hydrophobic. The transposon sequences that surround the gene encoding this CS(2) 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 CS(2) metabolism.