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Homocysteine, a non-protein amino acid, is an important risk factor for ischemic heart disease and stroke in humans. This review provides an overview of homocysteine influence on endothelium function as well as on protein metabolism with a special respect to posttranslational modification of protein with homocysteine thiolactone. Homocysteine is a pro-thrombotic factor, vasodilation impairing agent, pro-inflammatory factor and endoplasmatic reticulum-stress inducer. Incorporation of Hcy into protein via disulfide or amide linkages (S-homocysteinylation or N-homocysteinylation) affects protein structure and function. Protein N-homocysteinylation causes cellular toxicity and elicits autoimmune response, which may contribute to atherogenesis.

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The insight provided by the authors of this special issue on bioeconomy give a reassuring sign of optimism, vitality and strong will to make bioeconomy a success story. Key to these advances will be inventing and shaping our future and the cooperation of people who will create new scientific and technological discoveries, developments and their implementation into industrial practice. The vibrant global megatrend bioeconomy is developing along various dimensions depending on natural and social conditions, economic development and political objectives. As value chains from producer countries and regions to their corresponding customers are interconnected globally and bioeconomies are diverse, constructive dialogues and agreed social consensus are therefore relevant worldwide. Mapping and engineering the uncharted territories of the molecular transformations, which are key to the bioeconomy, represents a great opportunity for the molecular and engineering sciences to bring in their important contributions. The development of smart bioeconomies needs excellence in science-based concepts, long-term support of innovative and mission-oriented research and a subtle equilibrium between science push and market and social pull. On the policy front, coherent and science-based policy decisions embracing bioeconomy and being consistent with each other are needed. From a global perspective, bioeconomy topics should be included in the international and national agendas on sustainable development goals.

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Homocysteine (Hcy)-thiolactone mediates a post-translational incorporation of Hcy into protein in humans. Protein N-homocysteinylation is detrimental to protein structure and function and is linked to pathophysiology of hyperhomocysteinemia observed in humans and experimental animals. The modification by Hcy-thiolactone can be detrimental directly by affecting the function of an essential lysine residue or indirectly by interfering with the function of other essential residues or cofactors. Previous work has shown that cytochrome c is very sensitive to Hcy-thiolactone, which causes formation of N-Hcy-cytochrome c multimers. However, it was unclear what sites in cytochrome c were prone to Hcy attachment and whether N-linked Hcy can affect the structure and redox function of cytochrome c. Here we show that 4 lysine residues (Lys8 or -13, Lys86 or -87, Lys99, and Lys100) of cytochrome c are susceptible to N-homocysteinylation. We also show that N-homocysteinylation of 1 mol of lysine/mol of protein affects the redox state of the heme ligand of cytochrome c by rendering it reduced. The modification causes subtle structural changes, manifested as increased resistance of the N-Hcy-cytochrome c to proteolysis by trypsin, chymotrypsin, and Pronase. However, no major secondary structure perturbations were observed as shown by circular dichroism spectroscopy. Our data illustrate how N-homocysteinylation can interfere with the function of heme-containing proteins.

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