Measurement of the oxidation‐reduction potentials of amicyanin and <i>c</i>‐type cytochromes from <i>Paracoccus denitrificans</i>

Gray, Kevin A.; Knaff, David B.; Husain, Mazhar; Davidson, Victor L.

doi:10.1016/0014-5793(86)81496-x

Cited by 66 publications

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“…More similar is cytochrome c-553i from P . denitriJicans, which is, however, also involved in methanol oxidation and is also much larger than the cytochrome c-553 described in the present paper Gray et al, 1986). Cytochrome c-553 of M .…”

Section: Discussioncontrasting

confidence: 54%

“…The amino acid composition of the cytochrome was determined as described previously (Beardmore- Gray et al, 1982). It is presented with the values for cytochrome cL (from Beardmore- Gray et al, 1983) given for comparison in parentheses (ND, not determined): Asx, 23 (24); Thr, 4 (14); Ser 1 (7); Glx, 20 (26); Pro, 8 (13); Gly, 19 (23); Ala, 24 (14); cys, ND (3); Val, 8 ( 5 ) ; Met, 3 (3); Ile, 4 (6); Leu, 11 (15); Tyr, 10 (6); Phe, 5 ( 5 ) ; His, 8 (7); Lys, 17 (13); Arg, 6 (4); Trp, ND (2).…”

Section: Purijication and Characterization Of Cytochrome C-553mentioning

confidence: 99%

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Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Day

Nunn²,

Anthony³

1990

Journal of General Microbiology

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Methylobacterium extorquens AM1 contains a novel c-type cytochrome, called cytochrome c-553, previously thought to be a precursor of the electron acceptor (cytochrome cL) for methanol dehydrogenase. Its amino acid composition and serological characteristics show that it has no structural relationship to cytochrome cL. It usually comprises less than 5% of the total c-type cytochromes. In a moxD mutant, which contains neither methanol dehydrogenase nor cytochrome cL, it comprises 30% of the soluble cytochrome and it has been purified and characterized from that mutant. Cytochrome c-553 is large ( M , 23000), acidic and monohaem, with a redox potential of 194 mV. It reacts rapidly and completely with CO but is not autoxidizable. It is not autoreducible, and it is not an electron acceptor from methanol dehydrogenase or methylamhe dehydrogenase, nor an important electron donor to the oxidase. It is able to accept electrons from cytochrome cL and to donate electrons to cytochrome cH. It is present in the soluble fraction (presumably periplasmic) and membrane fraction of wild-type bacteria during growth on a wide range of growth substrates, but its function in these bacteria or in the moxD mutant has not been determined.

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Section: Discussioncontrasting

confidence: 54%

Section: Purijication and Characterization Of Cytochrome C-553mentioning

confidence: 99%

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Day

Nunn²,

Anthony³

1990

Journal of General Microbiology

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“…Cytochrome c551i does not accept electrons directly from free MADH or from free amicyanin (Gray et al, 1986). Furthermore, MADH-dependent reduction of the cytochrome is only observed in the TRP-A 'COOH presence of amicyanin.…”

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confidence: 94%

Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c‐type cytochrome

et al. 1993

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A ternary electron transfer protein complex has been crystallized and a preliminary structure investigation has been carried out. The complex is composed of a quinoprotein, methylamine dehydrogenase (MADH), a blue copper protein, amicyanin, and a C-type cytochrome All three proteins were isolated from Paracoccus denitrificans. The crystals of the complex are orthorhombic, space group C2221 with cell dimensions a = 148.81 A , b = 68.85 A, and c = 187.18 A . Two types of isomorphous crystals were prepared: one using native amicyanin and the other copper-free apo-amicyanin. The diffraction data were collected at 2.75 A resolution from the former and at 2.4 A resolution from the latter. The location of the MADH portion was determined by molecular replacement. The copper site of the amicyanin molecule was located in an isomorphous difference Fourier while the iron site of the cytochrome was found in an anomalous difference Fourier. The MADH from P. denitrificans (PD-MADH) is an H,L, hetero-tetramer with the H subunit containing 373 residues and the L subunit 131 residues, the latter containing a novel redox cofactor, tryptophan tryptophylquinone (TTQ). The amicyanin of P. denitrificans contains 105 residues and the cytochrome cg5li contains 155 residues. The ternary complex consists of one MADH tetramer with two molecules of amicyanin and two of Cssli, forming a hetero-octamer; the octamer is located on a crystallographic diad. The relative positions of the three redox centers-i.e., the TTQ of MADH, the copper of amicyanin, and the heme group of are presented. ., 1983). The crystal structures of MADH from both Thiobucillus versutus (Vellieux et al., 1989) and P. denitrifcuns (Chen et al., 1992b) have been determined, based on an X-ray sequence for the former. The structure of the latter has recently been rebuilt using the DNA-derived amino acid sequence (Chistoserdov et al., 1992) and refined at 1.75 A resolution (Chen et al., in prep.).The nature of the redox cofactor of MADH has been a challenging topic over the last decade. Recently a cofactor model was proposed for MADH based on biophysical studies and on the gene sequence of the L subunit of MADH. This new cofactor, 147

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“…When grown on methylamine as a sole source of carbon and energy, Paracoccus denitrificans synthesizes a methylamine dehydrogenase which functions in the periplasm of this gramnegative bacterium and donates electrons to a periplasmic type I blue copper protein, amicyanin (16). We have previously reported the partial purification of methylamine dehydrogenase from P. denitrificans (16) and have characterized the physical and redox properties of amicyanin (14,16,18,25) and periplasmic c-type cytochromes (14, 17) which accept electrons from methylamine dehydrogenase via amicyanin. This paper reports a relatively simple procedure by which methylamine dehydrogenase was purified to homogeneity from P. denitrificans and describes several of the physical and kinetic properties of this enzyme.…”

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confidence: 99%

Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans

Husain¹,

Davidson²

1987

J Bacteriol

110

106

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Methylamine dehydrogenase from Paracoccus denitrificans was purified to homogeneity in two steps from the periplasmic fraction of methylamine-grown cells. The enzyme exhibited a pI value of 4.3 and was composed of two 46,700-dalton subunits and two 15,500-dalton subunits. Each small subunit possessed a covalently bound pyrrolo-quinoline quinone prosthetic group. The amino acid compositions of the large and small subunits are very similar to those of other methylamine dehydrogenases which have been isolated from taxonomically different sources. It has been established recently that certain oxidoreductases from a variety of sources contain pyrrolo-quinoline quinone (PQQ) as a prosthetic group (2, 4, 10, 11). These quinoproteins include bacterial methanol (9) and glucose dehydrogenases (12), which possess noncovalently associated PQQ, and bacterial methylamine dehydrogenase, which contains a covalently bound form of PQQ (8,21). Mammalian plasma amine oxidase (26) and choline dehydrogenase (3) also possess covalently attached PQQ. When grown on methylamine as a sole source of carbon and energy, Paracoccus denitrificans synthesizes a methylamine dehydrogenase which functions in the periplasm of this gramnegative bacterium and donates electrons to a periplasmic type I blue copper protein, amicyanin (16). We have previously reported the partial purification of methylamine dehydrogenase from P. denitrificans (16) and have characterized the physical and redox properties of amicyanin (14,16,18,25) and periplasmic c-type cytochromes (14, 17) which accept electrons from methylamine dehydrogenase via amicyanin. This paper reports a relatively simple procedure by which methylamine dehydrogenase was purified to homogeneity from P. denitrificans and describes several of the physical and kinetic properties of this enzyme. MATERIALS AND METHODSBacterial strains and culture conditions. P. denitrificans (ATCC 13543) was grown aerobically at 30°C in the medium of Kornberg and Morris (23), supplemented with 0.05% NaHCO3, 0.01% yeast extract, and 0.5% methylamine, 0.5% methanol, or 0.3% succinate.Preparation of proteins. Methylamine dehydrogenase was purified from the periplasmic fraction of methylamine-grown cells, which was prepared by the method of Alefounder and Ferguson (1). Routinely, 15 to 20 g (wet weight) of cells was * Corresponding author. fractionated at a time, and four such preparations were pooled, concentrated by ultrafiltration over an Amicon YM5 membrane (Amicon Corp., Lexington, Mass.), dialyzed against 20 mM potassium phosphate (pH 7.2), and applied to a DEAE-cellulose column (3.5 by 30 cm) which had been equilibrated in the same buffer that was used for dialysis. This column was eluted with a linear gradient (2.0 liters) of 0 to 400 mM NaCl in the starting buffer. Fractions containing methylamine dehydrogenase were pooled, concentrated by ultrafiltration over an Amicon PM 30 membrane, dialyzed against 20 mM potassium phosphate (pH 7.2), and applied to a DEAE-Trisacryl (LKB Instruments, Inc., Rockville, Md.) column...

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Measurement of the oxidation‐reduction potentials of amicyanin and c‐type cytochromes from Paracoccus denitrificans

Cited by 66 publications

References 13 publications

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c‐type cytochrome

Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans

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