The structure of a P450 ω‐hydroxylase bound to its fatty acid product was determined, which revealed a narrow substrate tunnel that leads to the heme. The introduction of an arginine side chain in proximity to the carboxyl group of the fatty acid led to a reduced KM value for dodecanoic acid, which suggests the importance of an anchoring point in the active site. An increase in the flexibility of the substrate recognition region was also engineered, which resulted in a threefold improved product formation.

Three different reductases have been fused to CYP153 monooxygenase from Marinobacter aquaeolei. The most promising candidate has been analysed in terms of its linker part, which connects the reductase with the haem domain through sequence alignment of the corresponding reductase family CYP116B. To improve the artificial fusion construct, the linker length has been varied, thereby only altering the non‐conserved middle part of the linker. This way seven artificial fusion constructs have been engineered, which varied in linker length between 11 and 32 amino acids (“natural” is 16). These variations showed a substantial impact on the fusion construct. The best mutant, extended by two amino acids, showed an improved activity (67 %), higher stability (67 % more active haem domain after 2 h) and a coupling efficiency of 94 % (55 % higher than before). Presented in this paper is an approach to find and optimise artificial fusion constructs for P450 monooxygenases.

In recent years the proliferation of a new technological evolution has aroused great interest from science and practice: social media. Subsuming different types of online applications where users can create, edit and share content, social media enables new forms of interaction with others. Organisations already recognise its relevance and start leveraging on it. Furthermore, organisations identify the role of service innovation as one major driver for economic growth and competitive advantage. Nevertheless, although social media affords organisations to interact with their customers, the potential for utilising it for improving their service innovation activities is almost unexploited yet. Therefore, this paper aims at providing a framework for supporting the use of social media affordances for service innovation. Its applicability is tested in the domain "government". Based on theoretical constructs a conceptual analysis is presented, tested in a specific domain and supplemented by potential future research and implications for theory and practice.

The native redox partners of many novel cytochrome P450 monooxygenases (CYPs) are unknown. Therefore, they are combined with non‐native redox partners to obtain catalytically active systems. Understanding the CYP‐redox partner interactions is the basis of successful protein engineering. Six redox partner interaction sites (RPISs) were identified by systematic literature, sequence, and structure analyses. All six RPISs are proposed to contribute to class II CYP‐redox partner interaction interface, whereas four and five contribute to the interaction interface in class I prokaryotic and mitochondrial CYPs, respectively. The significance of the identified RPISs was tested by designing seven variants of CYP153 A (class I) as a fusion protein with its non‐native redox partner CYP102 A1 reductase (class II) and measuring electron coupling efficiencies with a precision of 1–3 %. The best variant K166Q had an improved electron coupling efficiency of 64 % as compared to 53 % for the wild type.

The front cover artwork for Issue 20/2016 is provided by researchers from the Universität Stuttgart (Germany) and the University of York (United Kingdom). The image shows a free fatty acid substrate which drops into the active site of a P450 enzyme in an aqueous solution. The fatty acid is kept in the splash through the specific structural elements of the enzyme. See the Full Paper itself at http://dx.doi.org/10.1002/cctc.201600680.