65 research outputs found
Resonance Raman spectra of the oxidized and reduced <i>Cc</i>PDH.
<p>From the top, oxidized form; reduced form prepared by addition of L-fucose; reduced form prepared with ascorbic acid. The measurements were carried out in 50 mM HEPES buffer, pH 7.0, at room temperature. The excitation wavelength and incident powers are 413.1 nm and 1 mW, respectively. All spectra were obtained with data accumulated over 30 sec with a spectral resolution of 1.47 cm<sup>-1</sup>.</p
Structure of d-glucosone (A) and l-fucose (B) in a <sup>1</sup>C<sub>4</sub> conformation.
<p>Structure of d-glucosone (A) and l-fucose (B) in a <sup>1</sup>C<sub>4</sub> conformation.</p
Specificity constant values of <i>Cc</i>PDH for various monosaccharides.
<p>Specificity constant values of <i>Cc</i>PDH for various monosaccharides.</p
UV-visible absorption spectra of <i>Cc</i>PDH.
<p>Black solid line, oxidized form; gray solid line, reduced form by addition of L-fucose; dotted line, reduced form prepared by addition of ascorbic acid. All spectra were recorded in 50 mM HEPES buffer, pH 7.0, at room temperature.</p
Vibrational frequencies (cm<sup>-1</sup>) of <i>Cc</i>PDH and cytochrome domain of CDH.
<p>Vibrational frequencies (cm<sup>-1</sup>) of <i>Cc</i>PDH and cytochrome domain of CDH.</p
Multiple alignments of the amino acid sequences of CBM1 of <i>Cc</i>PDH and other known CBM1s.
<p>Residues in bold are highly conserved and those in boxes with a black background are perfect matches. Aromatic residues that are candidates for carbohydrate binding are indicated by a filled arrow, and two pairs of cysteines forming disulfide bonds are indicated by filled and open circles, respectively. <i>Tr</i>CBHI, cellobiohydrolase I (Cel7A) from <i>Trichoderma reesei</i> (accession no. P62694); <i>Pc</i>CBHII, cellobiohydrolase II (Cel6A) from <i>Phanerochaete chrysosporium</i> (Q02321); <i>Pc</i>BGL3A, glucan β-1,3-glucosidase (Bgl) from <i>P</i>. <i>chrysosporium</i> (Q8TGC6); <i>Pc</i>CBHI, cellobiohydrolase I-2 (Cel7D) from <i>P</i>. <i>chrysosporium</i> (Q09431); <i>Tr</i>CBHII, cellobiohydrolase II (Cel6A) from <i>T</i>. <i>reesei</i> (P07987); <i>Pc</i>CBCytb562, carbohydrate-binding cytochrome <i>b</i><sub>562</sub> from <i>P</i>. <i>chrysosporium</i> (Q66NB8); <i>Mt</i>CDH, cellobiose dehydrogenase from <i>Myceliophthora thermophila</i> (O74240).</p
UV-visible absorption spectra of the apo- and holo-forms of DH<sub>PDH</sub>.
<p>Dotted line, apo-form of DH<sub>PDH</sub>; black solid line, holo-form of DH<sub>PDH</sub>; blue solid line, reduced form by addition of 1 mM l-fucose. All spectra were recorded in 50 mM HEPES buffer, pH 7.0 at room temperature.</p
Adsorption parameters of <i>Cc</i>PDH for highly crystalline celluloses from <i>Cladophora</i> and PASC.
<p>Adsorption parameters of <i>Cc</i>PDH for highly crystalline celluloses from <i>Cladophora</i> and PASC.</p
Fruiting body of <i>Coprinopsis cinerea</i>.
<p>Fruiting body of <i>Coprinopsis cinerea</i>.</p
Domain organization of <i>Cc</i>SDH, CDH from <i>P. chrysosporium</i>, CBM1-carrying CDH from <i>T. heterothallica</i>, and cellulose-binding cytochrome <i>b</i><sub>562</sub> from <i>P. chrysosporium</i>.
<p>Abbreviations: AA3, Auxiliary Activities (AA) family 3 enzymes defined as flavoproteins containing a flavin-adenine dinucleotide (FAD)-binding domain; AA8, AA family 8 enzymes with the cytochrome domain of spectral class <i>b</i>; CBM1, family 1 carbohydrate-binding module.</p
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