Remembering Heinrich Wieland (1877–1957) portrait of an organic chemist and founder of modern biochemistry

@article{Witkop1992RememberingHW,
  title={Remembering Heinrich Wieland (1877–1957) portrait of an organic chemist and founder of modern biochemistry},
  author={Bernhard Witkop},
  journal={Medicinal Research Reviews},
  year={1992},
  volume={12}
}
  • B. Witkop
  • Published 1 May 1992
  • Chemistry
  • Medicinal Research Reviews
The Woodward Research Institute, Robert Burns Woodward (1917–1979) and Chemistry behind the Glass Door
Certainly a highlight in the career of Nobel Laureate Professor Robert Burns Woodward (1917–1979) was the foundation of the Woodward Research Institute (WRI) at Ciba AG in Basel, Switzerland, in
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A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
TLDR
This appears to be the only example of two cross-linked, modified amino acyl residues having a functional role in the active site of an enzyme, in the absence of other cofactors or metal ions.
Mammalian alkaloids : synthesis and O-methylation of (S)- and (R)-3'-hydroxycoclaurine and their N-methylated analogues with S-adenosyl-L-[methyl-14C]methionine in presence of mammalian catechol O-methyltransferase
O-Methylation of the optically active 3′-hydroxycoclaurines 3a and 3b and of the N-methylated analogs 5a,b with S-adenosyl-L-[methyl-14C]methionine in presence of mammalian COMT was investigated in
Quinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone.
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  • Biology, Chemistry
    European journal of biochemistry
  • 1991
TLDR
It appears that a novel class of amino-acid-derived cofactors is emerging, ranging from the free radical form of tyrosine and tryptophan to those containing a dicarbonyl group (like the already known pyryvoyl group and the o-quinones here described).
A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase.
TLDR
The result indicates that, contrary to previous proposals, pyrroloquinoline quinone is not the active site cofactor in mammalian copper amine oxidases, and suggests that this compound has a functional role at an enzyme active site.
Guest-responsive structural changes in cholic acid intercalation crystals
CHOLIC acid forms multimolecular inclusion compounds with a variety of organic substances1. Some of these inclusion compounds have crystal structures containing channels2, which can perform efficient
Mammalian Alkaloids: O‐Methylation of (±)‐Norcoclaurine‐1‐carboxylic Acid and Related Isoquinolines Including (S)‐ and (R)‐Norcoclaurine with 14C‐Labeled S‐Adenosyl‐L‐Methionine in Presence of Mammalian Catechol O‐Methyltransferase
TLDR
(±)-Norcoclaurine-1-carboxylic acid and the derived dihydroisoquinolinone 6 afforded, on methylation with 14C-labeled S-adenosyl-L-methionine in the presence of mammalian catechol O-methyltransferase, exclusively the 7-O-methylated congeners 7 and 9.
Publishing by--and for?--the numbers.
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