Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace
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DOI: 10.1038/s41598-020-73266-y
Abstract: Lytic polysaccharide monooxygenase (LPMO) and copper binding protein CopC share a similar mononuclear copper site. This site is defined by an N-terminal histidine and a second internal histidine side chain in a configuration called the… read more here.
Keywords: evidence copper; biochemical evidence; copper; histidine brace ... See more keywords
Mapping the protonation states of the histidine brace in an AA10 lytic polysaccharide monooxygenase using CW-EPR spectroscopy and DFT calculations.
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DOI: 10.1039/d1fd00068c
Abstract: The active site of the polysaccharide-degrading lytic polysaccharide monooxygenase (LPMO) enzyme features a single copper ion coordinated by a histidine brace. The primary coordination sphere of the copper contains several ligating atoms which are bonded… read more here.
Keywords: lytic polysaccharide; aa10; histidine brace; spectroscopy ... See more keywords
Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications
Sign Up to like & getrecommendations! Published in 2021 at "Biochemical Society Transactions"
DOI: 10.1042/bst20201031
Abstract: Lytic polysaccharide monooxygenases (LPMOs) are mononuclear copper enzymes that catalyse the oxidative cleavage of glycosidic bonds. They are characterised by two histidine residues that coordinate copper in a configuration termed the Cu-histidine brace. Although first… read more here.
Keywords: histidine brace; polysaccharide monooxygenases; lytic polysaccharide; copper ... See more keywords