@article{StrippDuffusFourmondetal.2022,
  author    = {Stripp, Sven T. and Duffus, Benjamin R. and Fourmond, Vincent and Leger, Christophe and Leimk{\"u}hler, Silke and Hirota, Shun and Hu, Yilin and Jasniewski, Andrew and Ogata, Hideaki and Ribbe, Markus W.},
  title     = {Second and outer coordination sphere effects in nitrogenase, hydrogenase, formate dehydrogenase, and CO dehydrogenase},
  series = {Chemical reviews : CR},
  volume    = {122},
  journal   = {Chemical reviews : CR},
  number    = {14},
  publisher = {American Chemical Society},
  address   = {Washington, DC},
  issn      = {0009-2665},
  doi       = {10.1021/acs.chemrev.1c00914},
  pages     = {11900 -- 11973},
  year      = {2022},
  abstract  = {Gases like H-2, N-2, CO2, and CO are increasingly recognized as critical feedstock in "green" energy conversion and as sources of nitrogen and carbon for the agricultural and chemical sectors. However, the industrial transformation of N-2, CO2, and CO and the production of H-2 require significant energy input, which renders processes like steam reforming and the Haber-Bosch reaction economically and environmentally unviable. Nature, on the other hand, performs similar tasks efficiently at ambient temperature and pressure, exploiting gas-processing metalloenzymes (GPMs) that bind low-valent metal cofactors based on iron, nickel, molybdenum, tungsten, and sulfur. Such systems are studied to understand the biocatalytic principles of gas conversion including N-2 fixation by nitrogenase and H-2 production by hydrogenase as well as CO2 and CO conversion by formate dehydrogenase, carbon monoxide dehydrogenase, and nitrogenase. In this review, we emphasize the importance of the cofactor/protein interface, discussing how second and outer coordination sphere effects determine, modulate, and optimize the catalytic activity of GPMs. These may comprise ionic interactions in the second coordination sphere that shape the electron density distribution across the cofactor, hydrogen bonding changes, and allosteric effects. In the outer coordination sphere, proton transfer and electron transfer are discussed, alongside the role of hydrophobic substrate channels and protein structural changes. Combining the information gained from structural biology, enzyme kinetics, and various spectroscopic techniques, we aim toward a comprehensive understanding of catalysis beyond the first coordination sphere.},
  language  = {en}
}