Читать книгу Bioinorganic Chemistry - Rosette M. Roat-Malone - Страница 4

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1 Chapter 1Figure 1.1 Dose‐response curve for elements.Figure 1.2 Common transition metal coordination geometries.Figure 1.3 Ligand field splitting for d electrons in various ligand fields....Figure 1.4 High‐spin and low‐spin electron configurations in an octahedral f...Figure 1.5 Electron configurations for high‐spin Cr(II) and Cu(II).Figure 1.6 Complexes obeying the 16‐e and 18‐e rule.Figure 1.7 (a) Rubredoxin. (b) [2Fe2S] cluster in ferredoxins. (c) [4Fe4S] c...Figure 1.8 Possible amino acid‐metal complexation structures found in metall...Figure 1.9 (a) Primary structure of a peptide chain. (b) Possible rotation a...Figure 1.10 Hydrogen bonding to form protein α‐helical and β‐pleated sheet s...Figure 1.11 Graphical representation of the Michaelis–Menten equation for no...Figure 1.12 Lineweaver–Burk plot for no inhibitor, competitive and noncompet...Figure 1.13 Watson–Crick base‐pairing in DNA.Figure 1.14 Complimentary antiparallel double‐stranded (ds) DNA (dsDNA).Figure 1.15 Orientations found in DNA helices.Figure 1.16 Schematic representation of replication, transcription, and tran...Figure 1.17 (a) Cas9 (green); crRNA (orange); tracrRNA (purple); PAM sequenc...Figure 1.18 Visualization of Cas9 ribonucleoprotein (RNP) from PDB 4UNS [24]...Figure 1.19 A ruthenium complex that can detect a DNA mismatch. PDB 4E1U dat...Figure 1.20 Cyclic voltammetry of wild‐type and mutant EndoIII from figure 6...Figure 1.21 Structures for counting electrons using 16‐ and 18‐electron rule.
2 Chapter 2Figure 2.1 Example of a People's Split Valence Basis Set.Figure 2.2 Structure of the binuclear center (BNC) of protein data bank (PDB...
3 Chapter 3Figure 3.1 Dioxygen bound to myoglobin heme. Visualization from reference [1...Figure 3.2 Heme protoporphyrin IX (heme b) as found in Hb, Mb, and some cyto...Figure 3.3 Quaternary structure protein data bank (PDB) 4HHB.Figure 3.4 T and R states for iron hemes in Hb.Figure 3.5 Heme group from PDBe 5M3L as determined by cryo‐electron microsco...Figure 3.6 Possible O₂‐binding modes in hemoglobin.Figure 3.7 Heme a in Cytochrome c Oxidase (CcO).Figure 3.8 CcO CuA, Heme a, and the binuclear center (BNC) as visualized wit...Figure 3.9 Cytochrome c oxidase catalytic cycle.Figure 3.10 Proposed O–O cleavage mechanism in heme‐copper oxidases (HCOs) w...Figure 3.11 Cytochrome c oxidase (CcO) catalytic center intermediates.Figure 3.12 H K and D channels in cytochrome c oxidase using PDB 1V54 data a...Figure 3.13 Cytochrome c oxidase (CcO) Model Compounds.Figure 3.14 Reaction of a CcO model compound illustrating homolytic dioxygen...Figure 3.15 Reaction of LS‐AN, a CcO model compound, with a phenol (PhOH)....Figure 3.16 Water molecules and the H‐bonding amino acid residue side chains...Figure 3.17 FeMo cofactor (M‐cluster) in the MoFe protein of nitrogenase as ...Figure 3.18 PDB 4WN9 FeMo cofactor used in QM/QM’ calculations by Rao et al....Figure 3.19 Lowe‐Thorneley cycle proposed by Rao et al. [71].Figure 3.20 Relative Gibbs free energies for the E4 state reaction path [71]...Figure 3.21 Distal, alternating, hybrid hydrogenation of N₂ to form NH_3.Figure 3.22 Pathways from the protein surface to nitrogenase's active site. ...Figure 3.23 Molybdenum complex producing NH₃ from N₂ [79]^.Figure 3.24 Reactions producing NH₃ from N_2.Figure 3.25 Reduction system for N₂ to NH_3.Figure 3.26 Fe–dinitrogen complex with Tp^Ph,Me ligands.Figure 3.27 Model complex with adamantane (Ad) substituents [91].Figure 3.28 Model complex with boron central atom.Figure 3.29 Hydrogen evolution from a nitrogenase functional model [93].Figure 3.30 P‐Cluster Model Compound.Figure 3.31 Starting materials for FeMo‐cofactor structural model from refer...Figure 3.32 FeMoco‐factor Model Compound.Figure 3.33 Active Site of copper–zinc superoxide dismutase (CuZnSOD).Figure 3.34 (a) CuZn SOD1 dimer PDB 1E9P. (b) CuZn SOD1 dimer PDB 1L3N.Figure 3.35 Proposed SOD3 Mechanism.Figure 3.36 Superoxide dismutase (SOD) Model Compound Ligands.Figure 3.37 (a) PDB 1MTY [110] active site in α subunit of MMOH (H₂O/OH⁻...Figure 3.38 (a) Possible Q (a diiron species) structures in the mechanism fo...Figure 3.39 Metal centers and visualization of pmoB, pmoA, and pmoC for PDB ...
4 Chapter 4Figure 4.1 Active Site of [NiFe] hydrogenase as visualized from PDB 5XLH [1]...Figure 4.2 Comparison [FeFe] hydrogenase with gamma oxygen versus gamma carb...Figure 4.3 [Fe]‐hydrogenase active site from the X‐ray crystallographic entr...Figure 4.4 PDB 4U9H [NiFe]‐hydrogenase active site.Figure 4.5 Catalytic cycle for [NiFe]‐hydrogenase.Figure 4.6 PDB 4UD6 Ni‐C form in the [NiFe]‐hydrogenase catalytic cycle illu...Figure 4.7 [NiFe]‐hydrogenase model compound.Figure 4.8 [NiFe]‐hydrogenase model compounds. (a) dppe = 1,2‐bis(diphenylph...Figure 4.9 Model compounds representing [NiFe]‐hydrogenase Ni‐L state (react...Figure 4.10 [NiFe]‐hydrogenase model compound illustrating H₂ cleavage at th...Figure 4.11 Possible proton pathways to the H‐cluster involving amino‐acid r...Figure 4.12 Amino‐acid network surrounding the 2Fe_H subcluster for the CpI^AD...Figure 4.13 [FeFe]‐hydrogenase model complexes that produce H_2.Figure 4.14 Proposed [Fe]‐hydrogenase catalytic cycle.Figure 4.15 [Fe]‐hydrogenase model compounds: (a) short‐lived model compound...Figure 4.16 Human carbonic anhydrase II (hCAII), PDB 1CA2.Figure 4.17 Hydrophilic water channel leading to the Zn²⁺ active site and hy...Figure 4.18 Methazolamide interaction at the hCA II active site PDB 5C8I [34...Figure 4.19 Trifluoro hydroxamate hCA II inhibitor at the active site PDB 1A...Figure 4.20 The nitrogen cycle.Figure 4.21 iNOS active site with substrate L‐arginine from PDB 1NOD [48].Figure 4.22 PDB 1M8D iNOS_ox with inhibitor chlorzoxazone from reference [44]...Figure 4.23 Inducible NOS inhibitors from reference [49].Figure 4.24 L‐arginine and amidine inactivators of iNOS from reference [45]....Figure 4.25 PDB 5VV5 active site of hnNOS with inhibitor bound [51].Figure 4.26 Siroheme‐[4Fe4S] cluster active site for CSNIR nitrite reductase...Figure 4.27 Hemes and types I and II copper centers found in various NO enzy...Figure 4.28 Cd₁NIR nitrite reductase visualized from PDB 1NIR [54].Figure 4.29 Type I and type II copper sites for the nitrite reductase enzyme...Figure 4.30 Copper complex catalyzing the reaction forming NO from nitrite i...Figure 4.31 Route 2 mechanism for NO(g) release in CuNIR nitrite reductase [...Figure 4.32 CuNIR model complexes studied in reference [60].Figure 4.33 Model complexes and reactions with NO(g) [64].
5 Chapter 5Figure 5.1 Reconfigurable DNA tripods (a) tripod design: each arm consists o...Figure 5.2 (a) An ssDNA scaffold hybridizes with staple and capture strands ...Figure 5.3 Three major motifs for building two‐ and three‐dimensional DNA na...Figure 5.4 Scaffold (long ssDNA) and staple (short ssDNA) used to create nan...Figure 5.5 (a) Biotin and (b) streptavidin as connectors for nucleic acids t...Figure 5.6 Response of a gold nanorod‐DNA origami template nanostructure to ...Figure 5.7 Sizes and shapes of some important nanomaterials and other matter...Figure 5.8 Formation of a hybrid nanogel system.Figure 5.9 (a) Sizes, shapes, and surface‐functionalized nanoparticles targe...Figure 5.10 Functionalizing ligands for inorganic nanoparticles.Figure 5.11 Anticancer agents delivered in single‐ and multi‐wall carbon nan...
6 Chapter 6Figure 6.1 Structures of platinum anticancer agents approved for clinical us...Figure 6.2 Platinum(II) compounds approved for use outside the United States...Figure 6.3 An antitumor active trans‐platinum(II) compounds BBR3464 (Triplat...Figure 6.4 Dickerson Dodecamer (DDD) in complex with Triplatin indicating ph...Figure 6.5 Disaccharide linkages in heparan sulfate (HS).Figure 6.6 (a) Phosphate clamp; (b) sulfate clamp; (c) phosphate–arginine fo...Figure 6.7 Antitumor drugs used in combination with platinum‐containing anti...Figure 6.8 The anticancer platinum(IV) prodrug mitaplatin.Figure 6.9 (a) Formation of the metal‐organic cage (MOC) (b) formation of th...Figure 6.10 Ruthenium(III) antitumor compounds NAMI‐A, KP1019, and NKP1339....Figure 6.11 X‐ray crystallographic structure of NAMI‐A reaction products wit...Figure 6.12 Ruthenium(II) half sandwich antitumor compounds RAED‐C and RAPTA...Figure 6.13 [RuCl₂(η⁶‐arene)(η¹‐S‐aroylthiourea)] anticancer active complexe...Figure 6.14 Cartoon representation of [RuCl₂(η⁶‐arene)(η¹‐S‐aroylthiourea)] ...Figure 6.15 Comparison of activity of Ir and Ru half‐sandwich complexes.Figure 6.16 (a) Ruthenium(II) and (b) Iridium(II) antitumor complexes.Figure 6.17 Ruthenium(II) and osmium(II) antitumor complexes.Figure 6.18 Osmium(II) antitumor complexesFigure 6.19 Gold and titanium antitumor compounds.Figure 6.20 Copper complexes in clinical trials.Figure 6.21 Bismuth drugs and drug components.Figure 6.22 Colloidal bismuth subcitrate (CBS).Figure 6.23 (a) Structure Cu‐only SodC from Mycobacterium tuberculosis, (b) ...Figure 6.24 Superoxide dismutase variants found in prokaryotic bacteria and ...Figure 6.25 MnSOD2 in Homo sapiens susceptible to nitration inactivation and...Figure 6.26 Drugs used in ALS treatment.Figure 6.27 X‐ray structures of ALS mutants. (a) Metal‐reconstituted CuZn SO...Figure 6.28 Riluzole and active riluzole‐triazole hybrid compounds.Figure 6.29 Drugs or potential drugs used in Menkes disease treatment.Figure 6.30 Drugs or potential drugs used in Wilson disease treatment.Figure 6.31 (a) Aβ_1–42 peptide dimer determined by cryo‐electron micro...Figure 6.32 Metal coordination spheres for (a) Cu(I)–Aβ peptide; (b) Cu(II)–...Figure 6.33 (a) copper chelator PBT2; (b) copper chelator gtsm; (c) copper c...Figure 6.34 Drugs used combination therapy with arsenic trioxide for treatme...Figure 6.35 (a–d) Vanadium compounds used in type 2 diabetes treatment; (e, ...

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