Electrochemical and enzymatic oxidation of 5-hydroxytryptophan

Humphries, Keith A.; Wrona, Monika Z.; Dryhurst, Glenn

doi:10.1016/0022-0728(93)85026-d

Cited by 19 publications

(21 citation statements)

References 20 publications

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“…(25). Second, a mauFp-cat transcriptional fusion provides the same level of Cmr in the mauF mutant as in the wild type (7,49 (14,31). The fact that a c-type cytochrome is required for synthesis of active MADH was observed by Oozeer et al (51).…”

Section: Gccgcgcgccgagacgscctgcaccaactgcgccc4p'agacwcogacctcactcatcacmentioning

confidence: 85%

Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants

et al. 1994

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The nucleotide sequence of the methylamine utilization (mau) gene region from Methylobacterium eatorquens AM1 was determined. Open reading frames for 11 genes (mauFBEDACJGLMN) were found, all transcribed in the same orientation. The mauB, mauA, and mauC genes encode the periplasmic methylamine dehydrogenase (MADH) large and small subunit polypeptides and amicyanin, respectively. The products of mauD, mauG, mauL, and mauM were also predicted to be periplasmic. The products of mauF, mauE, and mauN were predicted to be membrane associated. The mauj product is the only polypeptide encoded by the mau gene cluster which is predicted to be cytoplasmic. Computer analysis showed that the MauG polypeptide contains two putative heme binding sites and that the MauM and MauN polypeptides have four and two FeS cluster signatures, respectively. Mutants generated by insertions in mauF, mauB, mauE, mauD, mau4, mauG, and mauL were not able to grow on methylamine or any other primary amine as carbon sources, while a mutant generated from an insertion in mauC was not able to utilize methylamine as a source of carbon but utilized C2 to C4 n-alkylamines as carbon sources. Insertion mutations in mauJ, mauM, and mauN did not impair the ability of the mutants to utilize primary n-alkylamines as carbon sources. All mau mutants were able to utilize methylamine as a nitrogen source, implying the existence of an alternative (methyl)amine oxidation system, and a low activity of N-methylglutamate dehydrogenase was detected. The mauD, mauE, and mauF mutants were found to lack the MADH small subunit polypeptide and have a decreased amount of the MADH large subunit polypeptide. In the mauG and mauL mutants, the MADH large and small subunit polypeptides were present at wild-type levels, although the MADHs in these strains were not functional. In addition, MauG has sequence similarity to cytochrome c peroxidase from Pseudomonas sp. The mauA, mauD, and mauE genes from Paracoccus denitrificans and the mauD and mauG genes from Methylophilus methylotrophus W3A1 were able to complement corresponding mutants of M. extorquens AM1, confirming their functional equivalence. Comparison of amino acid sequences of polypeptides encoded by mau genes from M. eorquens AM1, P. denitrifwcans, and ThiobaciUlus versutus shows that they have considerable similarity.

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Section: Gccgcgcgccgagacgscctgcaccaactgcgccc4p'agacwcogacctcactcatcacmentioning

confidence: 85%

Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants

et al. 1994

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“…5) show that the core of the MauG protein must be closely related in conformation to the core of the cytochrome c peroxidases and this includes conservatism in the active site residues at the distal surface of the P haem. Peroxidase activity has been shown to mediate cross-linking of free indole groups [41,42]. A tryptophan tyrosine cross link could be formed as a result of peroxidase activity of a mutant form of yeast cytochrome c peroxidase [43].…”

Section: The Maug Proteinsmentioning

confidence: 98%

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases

Pettigrew

Echalier

Pauleta

2006

Journal of Inorganic Biochemistry

100

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“…The translated amino acid sequences of mauG indicate that the genes encode for periplasmic bacterial cytochrome c peroxidases with molecular masses of 38.2 and 37.3 kDa for M. extorquens AM1 and M. methylotrophus W3A1-NS, respectively (Lidstrom and Chistoserdov 1993;Chistoserdov et al 1994a). Phenotypic characterization of mauG mutants in M. extorquens AM1 and sequence similarity with the bacterial cytochrome c peroxidase from Pseudomonas aeruginosa (Rönnberg 1987a, b) indicated that the mauG gene product may function in the synthesis of the Trp-Trp bond in tryptophan tryptophylquione (Dischia et al 1991;Humphries et al 1993;Lidstrom and Chistoserdov 1993; Van der Palen et al 1995), which is the cofactor in methylamine dehydrogenase (McIntire et al 1991).…”

Section: Introductionmentioning

confidence: 97%

Cytochrome c peroxidase from Methylococcus capsulatus Bath

Zahn

Arciero

Hooper

et al. 1997

Archives of Microbiology

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A bacterial cytochrome c peroxidase was purified from the obligate methanotroph Methylococcus capsulatus Bath in either the fully oxidized or the half reduced form depending on the purification procedure. The cytochrome was a homo-dimer with a subunit mol mass of 35.8 kDa and an isoelectric point of 4.5. At physiological temperatures, the enzyme contained one high-spin, low-potential (Em7 = -254 mV) and one low-spin, high-potential (Em7 = +432 mM ) heme. The low-potential heme center exhibited a spin-state transition from the penta-coordinated, high-spin configuration to a low-spin configuration upon cooling the enzyme to cryogenic temperatures. Using M. capsulatus Bath ferrocytochrome c555 as the electron donor, the KM and Vmax for peroxide reduction were 510 +/- 100 nM and 425 +/- 22 mol ferrocytochrome c555 oxidized min-1 (mole cytochrome c peroxidase)-1, respectively.

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Electrochemical and enzymatic oxidation of 5-hydroxytryptophan

Cited by 19 publications

References 20 publications

Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants

Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases

Cytochrome c peroxidase from Methylococcus capsulatus Bath

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