@article{goralski_emerging_2022,
	title = {Emerging artificial metalloenzymes for asymmetric hydrogenation reactions},
	volume = {66},
	issn = {13675931},
	url = {https://doi.org/10.1016/j.cbpa.2021.102096},
	doi = {10.1016/j.cbpa.2021.102096},
	abstract = {Artificial metalloenzymes (ArMs) utilize the best properties of homogenous transition metal catalysts and naturally occurring proteins. While synthetic metal complexes offer high tunability and broad-scope reactivity with a variety of substrates, enzymes further endow these complexes with enhanced aqueous stability and stereoselectivity. For these reasons, dozens of ArMs have been designed to perform catalytic asymmetric hydrogenation reactions, and hydrogenase ArMs are, in fact, the oldest class of ArMs. Herein, we report recent advances in the design of hydrogenase ArMs, including (i) the modification of natural [Fe]-hydrogenase by insertion of artificial metallocofactors, (ii) design of a novel ArM system from the tractable and inexpensive protein β-lactoglobulin to afford a high-performing transfer hydrogenase, and (iii) the design of chimeric streptavidin scaffolds that drastically alter the secondary coordination sphere of previously reported streptavidin/biotin transfer hydrogenase ArMs.},
	journal = {Current Opinion in Chemical Biology},
	author = {Goralski, Sean T. and Rose, Michael J.},
	year = {2022},
	note = {Publisher: Elsevier Ltd},
	pages = {102096},
}

{"_id":"ZAj2pmGXbu7XfQE83","bibbaseid":"goralski-rose-emergingartificialmetalloenzymesforasymmetrichydrogenationreactions-2022","author_short":["Goralski, S. T.","Rose, M. J."],"bibdata":{"bibtype":"article","type":"article","title":"Emerging artificial metalloenzymes for asymmetric hydrogenation reactions","volume":"66","issn":"13675931","url":"https://doi.org/10.1016/j.cbpa.2021.102096","doi":"10.1016/j.cbpa.2021.102096","abstract":"Artificial metalloenzymes (ArMs) utilize the best properties of homogenous transition metal catalysts and naturally occurring proteins. While synthetic metal complexes offer high tunability and broad-scope reactivity with a variety of substrates, enzymes further endow these complexes with enhanced aqueous stability and stereoselectivity. For these reasons, dozens of ArMs have been designed to perform catalytic asymmetric hydrogenation reactions, and hydrogenase ArMs are, in fact, the oldest class of ArMs. Herein, we report recent advances in the design of hydrogenase ArMs, including (i) the modification of natural [Fe]-hydrogenase by insertion of artificial metallocofactors, (ii) design of a novel ArM system from the tractable and inexpensive protein β-lactoglobulin to afford a high-performing transfer hydrogenase, and (iii) the design of chimeric streptavidin scaffolds that drastically alter the secondary coordination sphere of previously reported streptavidin/biotin transfer hydrogenase ArMs.","journal":"Current Opinion in Chemical Biology","author":[{"propositions":[],"lastnames":["Goralski"],"firstnames":["Sean","T."],"suffixes":[]},{"propositions":[],"lastnames":["Rose"],"firstnames":["Michael","J."],"suffixes":[]}],"year":"2022","note":"Publisher: Elsevier Ltd","pages":"102096","bibtex":"@article{goralski_emerging_2022,\n\ttitle = {Emerging artificial metalloenzymes for asymmetric hydrogenation reactions},\n\tvolume = {66},\n\tissn = {13675931},\n\turl = {https://doi.org/10.1016/j.cbpa.2021.102096},\n\tdoi = {10.1016/j.cbpa.2021.102096},\n\tabstract = {Artificial metalloenzymes (ArMs) utilize the best properties of homogenous transition metal catalysts and naturally occurring proteins. While synthetic metal complexes offer high tunability and broad-scope reactivity with a variety of substrates, enzymes further endow these complexes with enhanced aqueous stability and stereoselectivity. For these reasons, dozens of ArMs have been designed to perform catalytic asymmetric hydrogenation reactions, and hydrogenase ArMs are, in fact, the oldest class of ArMs. Herein, we report recent advances in the design of hydrogenase ArMs, including (i) the modification of natural [Fe]-hydrogenase by insertion of artificial metallocofactors, (ii) design of a novel ArM system from the tractable and inexpensive protein β-lactoglobulin to afford a high-performing transfer hydrogenase, and (iii) the design of chimeric streptavidin scaffolds that drastically alter the secondary coordination sphere of previously reported streptavidin/biotin transfer hydrogenase ArMs.},\n\tjournal = {Current Opinion in Chemical Biology},\n\tauthor = {Goralski, Sean T. and Rose, Michael J.},\n\tyear = {2022},\n\tnote = {Publisher: Elsevier Ltd},\n\tpages = {102096},\n}\n\n\n\n","author_short":["Goralski, S. T.","Rose, M. J."],"key":"goralski_emerging_2022-1","id":"goralski_emerging_2022-1","bibbaseid":"goralski-rose-emergingartificialmetalloenzymesforasymmetrichydrogenationreactions-2022","role":"author","urls":{"Paper":"https://doi.org/10.1016/j.cbpa.2021.102096"},"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/FRGBergamini","dataSources":["o2mL7kG99iAQPpNRJ"],"keywords":[],"search_terms":["emerging","artificial","metalloenzymes","asymmetric","hydrogenation","reactions","goralski","rose"],"title":"Emerging artificial metalloenzymes for asymmetric hydrogenation reactions","year":2022}