Methylamine dehydrogenase

A binary complex of MADH and amicyanin (Chen et al., 1992) and a ternary protein complex of these proteins plus cytochrome c-551i (Chen et al., 1994) from P. denitrificans have been crystallized and their structures have been determined. The structures of the crystallized complexes of these proteins indicate that the interface between MADH and amicyanin is 

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KA Gray, VL Davidson, DB Knaff. Complex formation between methylamine dehydrogenase and amicyanm from Paracocuus demtnficans. J Biol Chem 263 13987-13990, 1988. 

The Methylamine Dehydrogenase Electron Transfer Chain C. Dennison, G. W. Canters, S. de Vries, E. Vijgenboom, and R. J. van Spanning... 

Figure 2.7. Expected temperature dependence (in the experimentally accessible temperature range) in regime IV in the context of Figure 2.5. Ground state tunnelling occurs in regime IV. The experimental data for methylamine dehydrogenase are apparendy linear in regime IV but, as noted in the text, this linearity will likely not extend to cryogenic temperatures.

Conversion of methanol into formaldehyde by methanol dehydrogenase. A complex array of genes is involved in this oxidation and the dehydrogenase contains pyrroloquinoline quinone (PQQ) as a cofactor (references in Ramamoorthi and Lidstrom 1995). Details of its function must, however, differ from that of methylamine dehydrogenase that also contains a quinoprotein—tryptophan tryptophylquinone (TTQ). 

The Methylamine Dehydrogenase Electron Transfer Chain C. Dennison, G. W. Canters,... 

Methylamine dehydrogenase of Methylophilus methylotro-phus, proton transfer from the methylamine adduct of tryptophan tryptophylquinone (TTQ) CHs-amine vs. CDs-amine, transient kinetics studies of H-transfer step, H/D IE 5-40 °C, Ah/Ad = 16.8 0.5, AH 42.2 1.1 (H), 43.2 1.8 (D) kJ/mol, rate constant unchanged. 

Metal-bound amino acid complexes, 206-209 Metal ions, in biological systems, 153—154 Methylamine dehydrogenase, 69—70 reaction diagram, 54/... 

METHYLAMINE DEHYDROGENASE AMINE OXIDASES AMINE SULFOTRANSFERASE Amino add acetyltransferase,... 

LYSYL OXIDASE METHANE MONOOXYGENASE METHIONINE y-LYASE METHYLAMINE DEHYDROGENASE... 

METHYLAMINE DEHYDROGENASE N-METHYLCLUTAMATE SYNTHASE METHYLAMINE DEHYDROGENASE RESONANCE RAMAN SPECTROSCOPY TOPAQUINONE... 

The blue protein from A. faecalis strain S-6, which was isolated as a requirement for transferring electrons to a copper-containing nitrite reductase, has since been shown to have sequence homology with proteins arbitrarily designated pseudoazurin by Ambler and Tobari (1985), from Achromobacter cycloclastes and from Pseudomonas AMI. [Pseudomonas AMI also produces amicyanin, which is the recipient of electrons from methylamine dehydrogenase, (see below)]. In A. cycloclastes reduced pseudoazurin donates electrons to a copper nitrite reductase (Liu et ai, 1986), as it does in A. faecalis. Ambler and Tobari (1985)... 

Although crystals have been reported for two amicyanins (Petratos et al., 1988b Lim et al., 1986), the type 1 blue protein, which is an electron acceptor for methylamine dehydrogenase (Tobari and Harada, 1981 van Houweligen et al., 1989), neither study has yet been completed. The structure of methylamine dehydrogenase from Thiobacillus versutus (not a copper protein) has recently been reported (Vellieux et al., 1989). The amicyanin from P. denitrificans has actually been cocrystallized with methylamine dehydrogenase (F. S. Mathews, personal communication. 

Figure 15-9 Stereoscopic view of the large domain (residues 1-383) of tri-methylamine dehydrogenase from a methylotrophic bacterium. The helices and 3 strands of the (aP)8 barrel are drawn in heavy lines as are the FMN (center) and the Fe4S4 iron-sulfur cluster at the lower right edge. The a/P loop to which it is bound is drawn with dashed lines. The 733-residue protein also contains two other structural domains. From Lim et al.150 Courtesy of F. S. Mathews.

Measurements of many kinds have been made between natural donor-acceptor pairs such as cytochrome c-cytochrome (y,161462 cytochrome c-cytochrome c peroxidase (Fig. 16-9),153163-166 trimethylamine dehy-drogenase-FMN to Fe4S4 center (Fig. 15-9),167 and methylamine dehydrogenase (TTQ radical)-amicya-nin (Cu2+).168 Designed metalloproteins are being studied as well.169 Femtosecond laser spectroscopy is providing a new approach.169,3... 

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