Design of Functional Metalloproteins
By Yi Lu, Natasha H. Yeung, Nathan A. Sieracki, Nicholas M. Marshall. Nature, 2009
632 citations recorded by the source corpus.
Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their variants, but also can result in new metalloenzymes for biotechnological and pharmaceutical applications. Although it is much more challenging to design metalloproteins than non-metalloproteins, much progress has been made in this area, particularly in functional design, owing to recent advances in areas such as computational and structural biology.
Subfields: Molecular Biology, Plant Science
View Paper: https://www.semanticscholar.org/paper/7f51fe094df18c800c090eb9ab77a9e02da58869
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In Molecular Biology
Citations in the corpus
- Functional soft materials from metallopolymers and metallosupramolecular polymers. (2011, background): “Nonetheless, the de novo design of proteins to have predetermined functions has experienced major recent advance”
- Artificial Metalloenzymes: Reaction Scope and Optimization Strategies. (2018, background): “Lu later designed a heme/non-heme FeB binding site in Mb by incorporating the L29H-F43H-V68E mutations.(294) The binding of Fe(II) in the new artificial enzyme (FeBMb) was supported by the crystal structure of Fe(II)-FeBMb, in which the non-heme iron was coordinated with three histidines, one O atom”