Recent advances in the design and optimization of artificial metalloenzymes

Recent advances in the design and optimization of artificial metalloenzymes. Morita, I. & Ward, T. R. Current Opinion in Chemical Biology, 81:102508, August, 2024.

Paper doi abstract bibtex

Embedding a catalytically competent transition metal into a protein scaffold affords an artificial metalloenzyme (ArM). Such hybrid catalysts display features that are reminiscent of both homogeneous and enzymatic catalysts. Pioneered by Whitesides and Kaiser in the late 1970s, this field of ArMs has expanded over the past two decades, marked by ever-increasing diversity in reaction types, cofactors, and protein scaffolds. Recent noteworthy developments include i) the use of earth-abundant metal cofactors, ii) concurrent cascade reactions, iii) synergistic catalysis, and iv) in vivo catalysis. Thanks to significant progress in computational protein design, ArMs based on de novo–designed proteins and tailored chimeric proteins promise a bright future for this exciting field.

@article{morita_recent_2024,
	title = {Recent advances in the design and optimization of artificial metalloenzymes},
	volume = {81},
	issn = {1367-5931},
	url = {https://www.sciencedirect.com/science/article/pii/S136759312400084X},
	doi = {10.1016/j.cbpa.2024.102508},
	abstract = {Embedding a catalytically competent transition metal into a protein scaffold affords an artificial metalloenzyme (ArM). Such hybrid catalysts display features that are reminiscent of both homogeneous and enzymatic catalysts. Pioneered by Whitesides and Kaiser in the late 1970s, this field of ArMs has expanded over the past two decades, marked by ever-increasing diversity in reaction types, cofactors, and protein scaffolds. Recent noteworthy developments include i) the use of earth-abundant metal cofactors, ii) concurrent cascade reactions, iii) synergistic catalysis, and iv) in vivo catalysis. Thanks to significant progress in computational protein design, ArMs based on de novo–designed proteins and tailored chimeric proteins promise a bright future for this exciting field.},
	urldate = {2024-10-04},
	journal = {Current Opinion in Chemical Biology},
	author = {Morita, Iori and Ward, Thomas R.},
	month = aug,
	year = {2024},
	keywords = {Artificial metalloenzymes, Transition metal catalysis, metal catalysis},
	pages = {102508},
}

Downloads: 0

{"_id":"j5aAhyvNWsjCbPbL5","bibbaseid":"morita-ward-recentadvancesinthedesignandoptimizationofartificialmetalloenzymes-2024","author_short":["Morita, I.","Ward, T. R."],"bibdata":{"bibtype":"article","type":"article","title":"Recent advances in the design and optimization of artificial metalloenzymes","volume":"81","issn":"1367-5931","url":"https://www.sciencedirect.com/science/article/pii/S136759312400084X","doi":"10.1016/j.cbpa.2024.102508","abstract":"Embedding a catalytically competent transition metal into a protein scaffold affords an artificial metalloenzyme (ArM). Such hybrid catalysts display features that are reminiscent of both homogeneous and enzymatic catalysts. Pioneered by Whitesides and Kaiser in the late 1970s, this field of ArMs has expanded over the past two decades, marked by ever-increasing diversity in reaction types, cofactors, and protein scaffolds. Recent noteworthy developments include i) the use of earth-abundant metal cofactors, ii) concurrent cascade reactions, iii) synergistic catalysis, and iv) in vivo catalysis. Thanks to significant progress in computational protein design, ArMs based on de novo–designed proteins and tailored chimeric proteins promise a bright future for this exciting field.","urldate":"2024-10-04","journal":"Current Opinion in Chemical Biology","author":[{"propositions":[],"lastnames":["Morita"],"firstnames":["Iori"],"suffixes":[]},{"propositions":[],"lastnames":["Ward"],"firstnames":["Thomas","R."],"suffixes":[]}],"month":"August","year":"2024","keywords":"Artificial metalloenzymes, Transition metal catalysis, metal catalysis","pages":"102508","bibtex":"@article{morita_recent_2024,\n\ttitle = {Recent advances in the design and optimization of artificial metalloenzymes},\n\tvolume = {81},\n\tissn = {1367-5931},\n\turl = {https://www.sciencedirect.com/science/article/pii/S136759312400084X},\n\tdoi = {10.1016/j.cbpa.2024.102508},\n\tabstract = {Embedding a catalytically competent transition metal into a protein scaffold affords an artificial metalloenzyme (ArM). Such hybrid catalysts display features that are reminiscent of both homogeneous and enzymatic catalysts. Pioneered by Whitesides and Kaiser in the late 1970s, this field of ArMs has expanded over the past two decades, marked by ever-increasing diversity in reaction types, cofactors, and protein scaffolds. Recent noteworthy developments include i) the use of earth-abundant metal cofactors, ii) concurrent cascade reactions, iii) synergistic catalysis, and iv) in vivo catalysis. Thanks to significant progress in computational protein design, ArMs based on de novo–designed proteins and tailored chimeric proteins promise a bright future for this exciting field.},\n\turldate = {2024-10-04},\n\tjournal = {Current Opinion in Chemical Biology},\n\tauthor = {Morita, Iori and Ward, Thomas R.},\n\tmonth = aug,\n\tyear = {2024},\n\tkeywords = {Artificial metalloenzymes, Transition metal catalysis, metal catalysis},\n\tpages = {102508},\n}\n\n\n\n","author_short":["Morita, I.","Ward, T. R."],"key":"morita_recent_2024-1","id":"morita_recent_2024-1","bibbaseid":"morita-ward-recentadvancesinthedesignandoptimizationofartificialmetalloenzymes-2024","role":"author","urls":{"Paper":"https://www.sciencedirect.com/science/article/pii/S136759312400084X"},"keyword":["Artificial metalloenzymes","Transition metal catalysis","metal catalysis"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/FRGBergamini","dataSources":["o2mL7kG99iAQPpNRJ"],"keywords":["artificial metalloenzymes","transition metal catalysis","metal catalysis"],"search_terms":["recent","advances","design","optimization","artificial","metalloenzymes","morita","ward"],"title":"Recent advances in the design and optimization of artificial metalloenzymes","year":2024}