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Color Plates

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Figures

Image of Color Plate 1 (chapter 2).

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Color Plate 1 (chapter 2).

The genomic adaptation to HMF stress. Expressions of selected genes of ethanologenic yeast are shown under a normal control condition (a) and HMF stress condition (b) from 0, 10, 30, 60, and 120 min after the treatment showing significantly induced (blue) and repressed (red) mRNA expression caused by the HMF stress on a defined medium. Yellow indicates mRNA equally expressed under different conditions. Varied colors between yellow and red or yellow and blue, as shown in a colored bar on the far right, indicate varied quantitative measurements of mRNA expression levels in a log scale. (Reprinted from Liu, 2006, with kind permission of Springer Science and Business Media.)

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 2 (chapter 8).

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Color Plate 2 (chapter 8).

Schematic diagram of the cellulosome. The type I dockerins mediate attachment of the catalytic subunits to the scaffoldin, which is comprised of nine cohesins, a cellulose-binding domain, a hydrophilic domain of unknown function (X), and a type II dockerin. The scaffoldin likewise binds through its type II dockerin domain to a type II cohesin-containing protein on the bacterial cell surface that is thought to anchor the complex through a series of three surface layer homology (SLH) domains. Reproduced from Volkman et al., 2004, with permission of John Wiley & Sons.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 3 (chapter 8).

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Color Plate 3 (chapter 8).

Ribbon diagram structure of the cohesin-binding surface of type I dockerin from (a) and a molecular surface representation from the same view (b). Reproduced from Lytle et al., 2001.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 4 (chapter 8).

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Color Plate 4 (chapter 8).

Structure comparison of (a) type I dockerin and (b) C-terminal domain of cardiac muscle troponin C. Reproduced from Lytle et al., 2001.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 5 (chapter 8).

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Color Plate 5 (chapter 8).

Structures of type I cohesin-dockerin complex (a and c) and type I dockerin in the complex (b). (a) Complex of wild-type (WT) dockerin from Xyn10B and cohesin 2 of CipA. (b) Dockerin of Xyn10B in the complex. (c) The superposition of the cohesin-dockerin complex (in orange) with its S45A-T46A mutant complex (in blue). In the mutant complex, helix-1 (containing Ser-11 and Thr-12) dominates binding, whereas in the WT complex, helix-3 (containing Ser-45 and Thr-46) plays a key role in ligand recognition. The second molecule of the mutant complex is represented by a light-gray ribbon. The Ca ions are depicted as spheres and colored orange (the WT complex) and light blue (the mutant). Reproduced from Carvalho et al., 2003, 2007, with permission from the National Academy of Sciences.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 6 (chapter 13).

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Color Plate 6 (chapter 13).

The Volta experiment in a freshwater pond. Reprinted from (Ferry and Kastead, 2007) with permission of the publisher.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 7 (chapter 20).

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Color Plate 7 (chapter 20).

[FeFe] hydrogenase from (Peters et al., 1998). Protein Data Bank ID 1feh. (A) Three-dimensional structure of the enzyme. The dinuclear FeFe active site, the three [4Fe4S] centers, and the [2Fe2S] center are coordinated in the same subunit. (B) Structure details of the active site. The hetero atoms from the prosthetic groups are represented as spheres, and the protein ligands are represented as sticks. Iron is in cyan, sulfur is in yellow, oxygen is in red, nitrogen is in blue, and carbon is in gray. DTMA, dithiomethyl amine.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 8 (chapter 20).

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Color Plate 8 (chapter 20).

[NiFe] hydrogenase from (Rousset et al., 1998). Protein Data Bank ID 1frf. (A) Three-dimensional structure of the enzyme. The dinuclear NiFe active site is coordinated in the large subunit, and the two [4Fe4S] centers and the [3Fe4S] center are coordinated in the small subunit. (B) Structure details of the active site. The hetero atoms from the prosthetic groups are represented as spheres, and the protein ligands are represented as sticks. Iron is in cyan, nickel is in dark blue, sulfur is in yellow, oxygen is in red, nitrogen is in blue, and carbon is in gray.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 9 (chapter 20).

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Color Plate 9 (chapter 20).

Iron-sulfur centers. (A) [4Fe4S] center and (B) [3Fe4S] center. The hetero atoms from the prosthetic groups are represented as spheres, and the protein ligands are represented as sticks. Iron is in cyan, sulfur is in yellow, oxygen is in red, nitrogen is in blue, and carbon is in gray.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 10 (chapter 20).

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Color Plate 10 (chapter 20).

Schematic view of the [NiFe] hydrogenase activity. The three-dimensional structure is from Volbeda et al. (Volbeda et al., 2002). Protein Data Bank ID 1yqw. The gas channel is represented as a wire mesh. The hetero atoms from the prosthetic groups are represented as spheres.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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Image of Color Plate 11 (chapter 20).

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Color Plate 11 (chapter 20).

Structure of the distal [4Fe4S] center (Rousset et al., 1998). Protein Data Bank ID 1frf. The hetero atoms are represented as spheres, and the protein ligands are represented as sticks. Iron is in cyan, sulfur is in yellow, oxygen is in red, nitrogen is in blue, and carbon is in gray.

Citation: Wall J, Harwood C, Demain A. 2008. Color Plates, In Bioenergy. ASM Press, Washington, DC.
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