Abstract Photoenzymatic catalysis facilitates stereoselective new‐to‐nature chemistry under mild conditions. In addition to the rational design of artificial photoenzymes, naturally occurring redox enzymes can be repurposed to promote photoredox catalysis in the chiral protein environment.
Cathleen Zeymer +2 more
exaly +7 more sources
Fine‐tuning ethanol oxidation pathway enzymes and cofactor PQQ coordinates the conflict between fitness and acetic acid production by Acetobacter pasteurianus [PDF]
Summary The very high concentrations required for industrial production of free acetic acid create toxicity and low pH values, which usually conflict with the host cell growth, leading to a poor productivity.
Ling Gao +3 more
doaj +4 more sources
A new model for the pro-PQQ cofactor of quinoprotein methylamine dehydrogenase
A model for the pro‐PQQ cofactor of Thiobacillus versutus methylamine dehydrogenase was fitted into a 2.25 Å resolution electron density distribution for this enzyme. This proposed model of pro‐PQQ consists of a tyrosine‐derived quinone indole bicyclic structure.
Vellieux, Frederic M.D., Hol, Wim G.J.
exaly +3 more sources
Evidence for PQQ as cofactor in 3,4-dihydroxyphenylalanine (dopa) decarboxylase of pig kidney [PDF]
Pig kidney 3,4‐dihydroxyphenylalanine (dopa) decarboxylase (EC 4.1.1.28) was purified to homogeneity. Treatment of the enzyme with phenylhydrazine (PH) according to a procedure developed for analysis of quinoproteins gave products which were identified as the hydrazone of pyridoxal phosphate (PLP) and the C(5)‐hydrazone of pyrroloquinoline quinone (PQQ)
R A Van Der Meer, J A Duine, B W Groen
exaly +4 more sources
Determination of PQQ in quinoproteins with covalently bound cofactor and in PQQ-derivatives [PDF]
Application of the so‐called hexanol extraction procedure for PQQ determination, originally based on detachment of the cofactor from quinoproteins and conversion into PQQ‐5,5‐dihexyl ketal, leads in several cases to a number of products due to uncontrollable esterification.
van der Meer, Robert A. +3 more
exaly +3 more sources
Abstract The objective of this work was to study the role of pyrroloquinolinequinone (PQQ) of Serratia sp. S119 strain in the maintenance of the bacterial redox state and in the early interaction with peanut. Lipid peroxidation and antioxidant enzymatic activities were analyzed in Serratia sp. S119 and in its PQQ minus mutant Serratia sp.
Eliana Bianucci +2 more
exaly +4 more sources
Phenylhydrazine as probe for cofactor identification in amine oxidoreductases Evidence for PQQ as the cofactor in methylamine dehydrogenase [PDF]
Homogeneous methylamine dehydrogenase (primary‐amine:(acceptor) oxidoreductase (deaminating), EC 1.4.99.3, MADH) from the bacterium Thiobacillus versutus was treated with the inhibitor phenylhydrazine (PH). Derivatization of the cofactor in MADH took place in a fast reaction to give compound I.
R A Van Der Meer +2 more
exaly +4 more sources
Pyrroloquinoline quinone (PQQ) is the organic cofactor in soybean lipoxygenase-1 [PDF]
Treatment of soybean lipoxygenase‐1 (SLO) with phenylhydrazine (PH) induced inactivation and a maximum (350 nm) in the absorption spectrum of the enzyme. To detach the product having this absorption maximum, proteolysis was required. The product appeared to be the C(5) phenylhydrazone of pyrroloquinoline quinone (PQQ).
van der Meer, Robert A. +1 more
exaly +3 more sources
Role of PQQ as a mammalian enzyme cofactor?
Leigh M. Felton, Chris Anthony
exaly +3 more sources
PQQ Supplementation and SARS-CoV-2 Spike Protein-Induced Heart Inflammation
SARS-CoV-2 spike protein-induced heart inflammation may originate from either COVID-19 infection or the administration of COVID-19 mRNA vaccines. As pyrroloquinoline quinone (PQQ) is a scavenger of free radicals, redox cofactor, and antioxidant which ...
Alberto Boretti
doaj +2 more sources

