Modelling a ‘histidine brace’ motif in mononuclear copper monooxygenases

2020 ◽  
Vol 56 (38) ◽  
pp. 5123-5126
Author(s):  
Arisa Fukatsu ◽  
Yuma Morimoto ◽  
Hideki Sugimoto ◽  
Shinobu Itoh
Keyword(s):  
Copper Complex ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Site Model ◽  
Lytic Polysaccharide Monooxygenases ◽  
Active Site Model ◽  
Polysaccharide Monooxygenases

A mononuclear copper complex bearing a ‘histidine brace’ is synthesised and characterised as an active-site model of mononuclear copper monooxygenases such as lytic polysaccharide monooxygenases (LPMOs) and particulate methane monooxygenase (pMMO).

Structural and Spectroscopic Features of acis(Hydroxo)-FeIII-(Carboxylato) Configuration as an Active Site Model for Lipoxygenases

2002 ◽  
Vol 41 (21) ◽  
pp. 5513-5520 ◽  
Author(s):  
Seiji Ogo ◽  
Ryo Yamahara ◽  
Mark Roach ◽  
Tomoyoshi Suenobu ◽  
Michihiko Aki ◽  
...  
Keyword(s):  
Active Site ◽  
Site Model ◽  
Active Site Model

Glutathione peroxidase: Redox chemistry of active site model peptides

1991 ◽  
Vol 1 (5) ◽  
pp. 277-280 ◽  
Author(s):  
P. Chan ◽  
P. Cotelle ◽  
N. Cotelle ◽  
J.L. Bernier ◽  
J.P. Hénichart
Keyword(s):  
Glutathione Peroxidase ◽  
Active Site ◽  
Redox Chemistry ◽  
Site Model ◽  
Active Site Model ◽  
Model Peptides

Recent insights into lytic polysaccharide monooxygenases (LPMOs)

2018 ◽  
Vol 46 (6) ◽  
pp. 1431-1447 ◽  
Author(s):  
Tobias Tandrup ◽  
Kristian E. H. Frandsen ◽  
Katja S. Johansen ◽  
Jean-Guy Berrin ◽  
Leila Lo Leggio
Keyword(s):  
Active Site ◽  
Room Temperature ◽  
Experimental Studies ◽  
Binding Mode ◽  
Structural Features ◽  
Oxygen Species ◽  
Animal Kingdom ◽  
X Ray ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases

Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes discovered within the last 10 years. By degrading recalcitrant substrates oxidatively, these enzymes are major contributors to the recycling of carbon in nature and are being used in the biorefinery industry. Recently, two new families of LPMOs have been defined and structurally characterized, AA14 and AA15, sharing many of previously found structural features. However, unlike most LPMOs to date, AA14 degrades xylan in the context of complex substrates, while AA15 is particularly interesting because they expand the presence of LPMOs from the predominantly microbial to the animal kingdom. The first two neutron crystallography structures have been determined, which, together with high-resolution room temperature X-ray structures, have putatively identified oxygen species at or near the active site of LPMOs. Many recent computational and experimental studies have also investigated the mechanism of action and substrate-binding mode of LPMOs. Perhaps, the most significant recent advance is the increasing structural and biochemical evidence, suggesting that LPMOs follow different mechanistic pathways with different substrates, co-substrates and reductants, by behaving as monooxygenases or peroxygenases with molecular oxygen or hydrogen peroxide as a co-substrate, respectively.

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