2011
DOI: 10.1073/pnas.1109423108
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Abstract: The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Catalysis proceeds through a high valent bis-Fe(IV) redox state and requires long-range electron transfer (ET), as the distance between the modified residues of pre-MADH and the nearest heme iron of MauG is 19.4 Å. Trp199 of MauG resides at the MauG-preMADH interface, positioned midway bet… Show more

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Cited by 62 publications
(101 citation statements)
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“…The W199F MauG mutant can form the bis-Fe(IV) state on reaction with H 2 O 2 , but cannot catalyze TTQ biosynthesis, as hole hopping through Trp199 is required for preTTQ oxidation ( Fig. S1A) (13,14). In contrast to the native MauG-preMADH crystals, the W199F MauG-preMADH crystals showed no changes at the preTTQ site after 60 d ( Fig.…”
Section: Resultsmentioning
confidence: 70%
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“…The W199F MauG mutant can form the bis-Fe(IV) state on reaction with H 2 O 2 , but cannot catalyze TTQ biosynthesis, as hole hopping through Trp199 is required for preTTQ oxidation ( Fig. S1A) (13,14). In contrast to the native MauG-preMADH crystals, the W199F MauG-preMADH crystals showed no changes at the preTTQ site after 60 d ( Fig.…”
Section: Resultsmentioning
confidence: 70%
“…S2D) (15). The other species present is 2-Da lighter (14,995.60 ± 0.05 Da) than β-pre-MADH in the control (14,997.54 ± 0.02 Da) and H 2 O 2 -treated samples (14,997.32 ± 0.26 Da; Fig. S2B), which is consistent with a β-MADH species containing the cross-link between βTrp57-OH and βTrp108 in the absence of the second oxygen atom.…”
Section: Resultsmentioning
confidence: 99%
“…3E). Both variants were shown to be capable of stabilizing the bis-Fe(IV) species (25,26). In contrast, the NIR spectral feature was not observed in Y294H MauG upon addition of H 2 O 2 ( Fig.…”
Section: Resultsmentioning
confidence: 89%
“…Thus, a hole-hopping mechanism for ET between the hemes mediated by Trp93 can explain the observed CR-transition phenomenon in bis-Fe(IV) MauG in the absence of direct contact between the hemes. It is interesting to note that ET via hole hopping also is suggested to occur between bis-Fe(IV) MauG and the tryptophan residues being oxidized in preMADH via a tryptophan residue located at the interface of the MauG-preMADH complex (25,40).…”
Section: Resultsmentioning
confidence: 99%
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