Results 121 to 130 of about 95,534 (148)

Substituted Quinoline Quinones as Surrogates for the PQQ Cofactor: An Electrochemical and Computational Study

Organic Letters, 2015
Pyrroloquinoline quinones (PQQ) are important cofactors that shuttle redox equivalents in diverse metalloproteins. Quinoline 7,8-quinones have been synthesized and characterized as surrogates for PQQ to elucidate redox energetics within metalloenzyme active sites.
Walter L, Dorfner, Patrick J, Carroll, Eric J, Schelter   +2 more
openaire   +3 more sources

First Experimental Structure of a 1:1 Metal Complex with a PQQ Cofactor Derivative outside Dehydrogenase Enzymes

Inorganic Chemistry, 1999
Qualitatively similar metal coordination as in PQQ-dependent bacterial dehydrogenases was observed for the PQQ triester in the model complex I, although the unusual five-coordinate copper(I) center...
Matthias Wanner, Torsten Sixt, Karl-Wilhelm Klinkhammer, Wolfgang Kaim   +3 more
openaire   +2 more sources

PQQ or TOPA? A theoretical suggestion for the organic cofactor of amine oxidases

Computational and Theoretical Chemistry, 1992
Abstract Bovine serum amine oxidase contains a quinoid cofactor which was first identified as PQQ (pyrroloquinoline quinone) and recently as TOPA, the oxidized form of 6-hydroxydopa. Theoretical ab initio and PPP calculations were performed on the two molecules. The comparison of the electronic spectrum of the enzyme and of its phenylhydrazine adduct
Laura Morpurgo
exaly   +2 more sources

Protein lysine 6-oxidase (lysyl oxidase) cofactor: Methoxatin (PQQ) or pyridoxal?

International Journal of Biochemistry & Cell Biology, 1988
1. Treatment of chick embryos with two lathyrogens lowered lysyl oxidase and increased collagen extractability. 2. Subsequent treatment with pyridoxal restored both parameters towards normal, whereas PQQ treatment was less effective. 3. These results suggest the requirement of a pyridoxal derivative for the formation of the enzyme, acting either as ...
C I, Levene, M P, O'Shea, M J, Carrington   +2 more
exaly   +3 more sources

Synthesis of Imidazolo Analogues of the Oxidation−Reduction Cofactor Pyrroloquinoline Quinone (PQQ)

The Journal of Organic Chemistry, 2004
Parallel syntheses of 2-hydro-, 2-methyl-, and 2-methoxycarbonylimidazo-7,9-dimethoxycarbonyl analogues of the oxidation-reduction cofactor pyrroloquinoline quinone [4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid] have been developed. The properties of the imidazolo analogues in relation to the corresponding pyrrole analogues
David M D, Fouchard, L M V, Tillekeratne, Richard A, Hudson   +2 more
openaire   +3 more sources

Lysyl oxidase (Protein lysine 6-oxidase) cofactor: Methoxatin (PQQ) or pyridoxal7

Pharmacological Research Communications, 1988
C I Levene
exaly   +2 more sources

Ambident Behavior of the“New Vitamin” Methoxatin(Cofactor PQQ) towards Metals: Coordinative Stabilization of the Pyrrolide Form and the Semiquinone Form

Angewandte Chemie International Edition in English, 1990
Brigitte Schwederski, Wolfgang Kaim
exaly   +2 more sources

Computational Study of Aromatic Hydroxylation Catalyzed by the Iron-Dependent Hydroxylase PqqB Involved in the Biosynthesis of Redox Cofactor Pyrroloquinoline Quinone.

Inorganic Chemistry, 2022
PqqB from Methylobacterium extorquens is a unique nonheme iron-dependent hydroxylase involved in the biosynthesis of redox cofactor pyrroloquinoline quinone (PQQ).
Yaru Liu, Yongjun Liu
semanticscholar   +1 more source

Pyrroloquinoline quinone (PQQ)

Textbook of Natural Medicine, 2020
Pyrroloquinoline quinone (PQQ) is a novel vitamin-like compound that acts as an essential active factor in the functioning of mitochondria. However, as higher organisms do not seem to biosynthesize PQQ, the major source in humans is the diet. In addition
Michaela Murray
semanticscholar   +1 more source

Biochemistry: role of PQQ as a mammalian enzyme cofactor?

Nature, 2005
The announcement by Kasahara and Kato of a new redox-cofactor vitamin for mammals, pyrroloquinoline quinone (PQQ), was based on their claim that an enzyme, predicted to be involved in mouse lysine metabolism, is a PQQ-dependent dehydrogenase. However, this claim was dependent on a sequence analysis using databases that inappropriately label beta ...
Leigh M, Felton, Chris, Anthony
openaire   +1 more source