Literature summary for 1.4.9.1 extracted from

Feng, M.; Ma, Z.; Crudup, B.F.; Davidson, V.L.
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 A away (2017), FEBS Lett., 591, 1566-1572 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
amicyanin	-	Paracoccus denitrificans
MauG	a diheme enzyme, the diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40A from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H2O2 both hemes become FeIV. In the absence of preMADH the hemes autoreduce to ferric heme in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance. MauG structure, PDB ID 3L4M. Kinetics overview	Paracoccus denitrificans

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of pre-MADH in Rhodobacter sphaeroides	Paracoccus denitrificans

Organism

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	P22619 AND P29894	alpha and beta subunits encoded by genes mauA and mauB	-

Synonyms

Synonyms	Comment	Organism
MADH	-	Paracoccus denitrificans

General Information

General Information	Comment	Organism
physiological function	the diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. Tinding of preMADH to MauG affects both the coordination state of the ferric high-spin heme, and the kinetic mechanism of the autoreduction of the bis-FeIV hemes. Binding sructure analysis, overview	Paracoccus denitrificans

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Release 2023.1 (January 2023)