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tryptophan tryptophylquinone

Known as: (2,4'-Bi-1H-indole)-3,3'-dipropanoic acid, alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-, 4-(2'-tryptophyl)tryptophan-6,7-dione, tryptophan-tryptophan quinone 
National Institutes of Health

Related topics

Related topics

3 relations

Broader (2)

IndolequinonesTryptophan
analogs & derivatives

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2012
2012
Effects of the loss of the axial tyrosine ligand of the low‐spin heme of MauG on its physical properties and reactivity
2011
2011
The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.
The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of… 
2010
2010
Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.
The diheme enzyme MauG catalyzes the post-translational modification of a precursor protein of methylamine dehydrogenase (preMADH… 
2010
2010
Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine .
The diheme enzyme MauG catalyzes the posttranslational modification of a precursor protein of methylamine dehydrogenase (preMADH… 
2005
2005
Active Site Aspartate Residues Are Critical for Tryptophan Tryptophylquinone Biogenesis in Methylamine Dehydrogenase*
The biosynthesis of methylamine dehydrogenase (MADH) requires formation of six intrasubunit disulfide bonds, incorporation of two… 
1998
1998
Methylamine dehydrogenase is a light-dependent oxidase.
1997
1997
Amine-oxidizing quinoproteins.
1995
1995
Spectroscopic Evidence for a Common Electron Transfer Pathway for Two Tryptophan Tryptophylquinone Enzymes (*)
Aromatic amine dehydrogenase (AADH) and methylamine dehydrogenase (MADH) are the only two enzymes known to use the cofactor… 
1995
1995
Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer.
Within the methylamine dehydrogenase-amicyanin complex, intermolecular electron transfer (ET) occurs between tryptophan… 
1993
1993
Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan…
Five mutants of Methylobacterium extorquens and four mutants of Paracoccus denitrificans that have a general defect in c-type… 
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