Cover -- Title Page -- Copyright -- Contents -- About the Editor -- List of Contributors -- Preface -- Acknowledgements -- Chapter 1 New Applications of Immobilized Metal Ion Affinity Chromatography in Chemical Biology -- 1.1 Introduction -- 1.2 Principles and Traditional Use -- 1.3 A Brief History -- 1.4 New Application 1: Non-protein Based Low Molecular Weight Compounds -- 1.4.1 Siderophores -- 1.4.2 Anticancer Agent: Trichostatin A -- 1.4.3 Anticancer Agent: Bleomycin -- 1.4.4 Anti-infective Agents -- 1.4.5 Other Agents -- 1.4.6 Selecting a Viable Target -- 1.5 New Application 2: Multi-dimensional Immobilized Metal Ion Affinity Chromatography -- 1.6 New Application 3: Metabolomics -- 1.7 New Application 4: Coordinate-bond Dependent Solid-phase Organic Synthesis -- 1.8 Green Chemistry Technology -- 1.9 Conclusion -- Acknowledgments -- References -- Chapter 2 Metal Complexes as Tools for Structural Biology -- 2.1 Structural Biological Studies and the Major Techniques Employed -- 2.2 What do Metal Complexes have to Offer the Field of Structural Biology? -- 2.3 Metal Complexes for Phasing in X-ray Crystallography -- 2.4 Metal Complexes for Derivation of Structural Restraints via Paramagnetic NMR Spectroscopy -- 2.4.1 Paramagnetic Relaxation Enhancement (PRE) -- 2.4.2 Residual Dipolar Coupling (RDC) -- 2.4.3 Pseudo-Contact Shifts (PCS) -- 2.4.4 Strategies for Introducing Lanthanide Ions into Bio-Macromolecules -- 2.5 Metal Complexes as Spin Labels for Distance Measurements via EPR Spectroscopy -- 2.6 Metal Complexes as Donors for Distance Measurements via Luminescence Resonance Energy Transfer (LRET) -- 2.7 Concluding Statements and Future Outlook -- References -- Chapter 3 AAS, XRF, and MS Methods in Chemical Biology of Metal Complexes -- 3.1 Introduction -- 3.2 Atomic Absorption Spectroscopy (AAS).

3.2.1 Fundamentals and Basic Principles of AAS -- 3.2.2 Instrumental and Technical Aspects of AAS -- 3.2.3 Method Development and Aspects of Practical Application -- 3.2.4 Selected Application Examples -- 3.3 Total Reflection X-Ray Fluorescence Spectroscopy (TXRF) -- 3.3.1 Fundamentals and Basic Principles of TXRF -- 3.3.2 Instrumental/Methodical Aspects of TXRF and Applications -- 3.4 Subcellular X-ray Fluorescence Imaging of a Ruthenium Analogue of the Malaria Drug Candidate Ferroquine Using Synchrotron Radiation -- 3.4.1 Application of X-ray Fluorescence in Drug Development Using Ferroquine as an Example -- 3.5 Mass Spectrometric Methods in Inorganic Chemical Biology -- 3.5.1 Mass Spectrometry and Inorganic Chemical Biology: Selected Applications -- 3.6 Conclusions -- Acknowledgements -- References -- Chapter 4 Metal Complexes for Cell and Organism Imaging -- 4.1 Introduction -- 4.2 Photophysical Properties -- 4.2.1 Fluorescence and Phosphorescence -- 4.2.2 Two-photon Absorption -- 4.2.3 Upconversion Luminescence -- 4.3 Detection of Luminescent Metal Complexes in an Intracellular Environment -- 4.3.1 Confocal Laser-scanning Microscopy -- 4.3.2 Fluorescence Lifetime Imaging Microscopy -- 4.3.3 Flow Cytometry -- 4.4 Cell and Organism Imaging -- 4.4.1 Factors Affecting Cellular Uptake -- 4.4.2 Organelle Imaging -- 4.4.3 Two-photon and Upconversion Emission Imaging for Cells and Organisms -- 4.4.4 Intracellular Sensing and Labeling -- 4.5 Conclusion -- Acknowledgements -- References -- Chapter 5 Cellular Imaging with Metal Carbonyl Complexes -- 5.1 Introduction -- 5.2 Vibrational Spectroscopy of Metal Carbonyl Complexes -- 5.3 Microscopy and Imaging of Cellular Systems -- 5.3.1 Techniques of Vibrational Microscopy -- 5.4 Infrared Microscopy.

5.4.1 Concentration Measurements with IR Spectroscopy and Spectromicroscopy -- 5.4.2 Water Absorption -- 5.4.3 Metal Carbonyls as IR Probes for Cellular Imaging -- 5.4.4 In Vivo Uptake and Reactivity of Metal Carbonyl Complexes -- 5.5 Raman Microscopy -- 5.5.1 Concentration Measurements with Raman Spectroscopy and Spectromicroscopy -- 5.5.2 Metal Carbonyls as Raman Probes for Cellular Imaging -- 5.6 Near-field Techniques -- 5.6.1 Concentration Measurements with Near-field Techniques -- 5.6.2 High-resolution Measurement of Intracellular Metal-Carbonyl Accumulation by Photothermal Induced Resonance -- 5.7 Comparison of Techniques -- 5.8 Conclusions and Outlook -- Acknowledgements -- References -- Chapter 6 Probing DNA Using Metal Complexes -- 6.1 General Introduction -- 6.2 Photophysics of Ru(II) Complexes -- 6.2.1 The First Ru(II) Complex Studied in the Literature: [Ru(bpy)3]2+ -- 6.2.2 Homoleptic Complexes -- 6.2.3 Heteroleptic Complexes -- 6.2.4 Photoinduced Electron Transfer (PET) and Energy Transfer Processes -- 6.3 State-of-the-art on the Interactions of Mononuclear Ru(II) Complexes with Simple Double-stranded DNA -- 6.3.1 Studies on Simple Double-stranded DNAs -- 6.3.2 Influence of DNA on the Emission Properties -- 6.4 Structural Diversity of the Genetic Material -- 6.4.1 Mechanical Properties of DNA -- 6.4.2 DNA Topology -- 6.4.3 SMF Study with [Ru(phen)2(PHEHAT)]2+ and [Ru(TAP)2(PHEHAT)]2+ -- 6.5 Unusual Interaction of Dinuclear Ru(II) Complexes with Different DNA Types -- 6.5.1 Reversible Interaction of [{(Ru(phen)2}2HAT]4+ with Denatured DNA -- 6.5.2 Targeting G-quadruplexes with Photoreactive [{Ru(TAP)2}2TPAC]4+ -- 6.5.3 Threading Intercalation -- 6.6 Conclusions -- Acknowledgement -- References.

Chapter 7 Visualization of Proteins and Cells Using Dithiol-reactive Metal Complexes -- 7.1 The Chemistry of As(III) and Sb(III) -- 7.2 Cysteine Dithiols in Protein Function -- 7.3 Visualization of Dithiols in Isolated Proteins with As(III) -- 7.4 Visualization of Dithiols on the Mammalian Cell Surface with As(III) -- 7.5 Visualization of Dithiols in Intracellular Proteins with As(III) -- 7.6 Visualization of Tetracysteine-tagged Recombinant Proteins in Cells with As(III) -- 7.7 Visualization of Cell Death in the Mouse with Optically Labelled As(III) -- 7.7.1 Cell Death in Health and Disease -- 7.7.2 Cell Death Imaging Agents -- 7.7.3 Visualization of Cell Death in Mouse Tumours, Brain and Thrombi with Optically Labelled As(III) -- 7.8 Visualization of Cell Death in Mouse Tumours with Radio-labelled As(III) -- 7.9 Summary and Perspectives -- References -- Chapter 8 Detection of Metal Ions, Anions and Small Molecules Using Metal Complexes -- 8.1 How Do We See What's in a Cell? -- 8.1.1 Why Metal Complexes as Sensors? -- 8.1.2 Design Strategies for Sensors Built with Metal Complexes -- 8.1.3 General Criteria of Metal-based Sensors for Bioimaging -- 8.2 Metal Complexes for Detection of Metal Ions -- 8.2.1 Tethered Sensors for Detecting Metal Ions -- 8.2.2 Displacement Sensors for Detecting Metal Ions -- 8.2.3 MRI Contrast Agents for Detecting Metal Ions -- 8.2.4 Chemodosimeters for Metal Ions -- 8.3 Metal Complexes for Detection of Anions and Neutral Molecules -- 8.3.1 Tethered Approach: Metal Complex as Recognition Unit -- 8.3.2 Displacement Approach: Metal Complex as Quencher -- 8.3.3 Dosimeter Approach -- 8.4 Conclusions -- Acknowledgements -- Abbreviations -- References -- Chapter 9 Photo-release of Metal Ions in Living Cells.

9.1 Introduction to Photochemical Tools Including Photocaged Complexes -- 9.2 Calcium Biochemistry and Photocaged Complexes -- 9.2.1 Strategies for Designing Photocaged Complexes for Ca2+ -- 9.2.2 Biological Applications of Photocaged Ca2+ Complexes -- 9.3 Zinc Biochemistry and Photocaged Complexes -- 9.3.1 Biochemical Targets for Photocaged Zn2+ Complexes -- 9.3.2 Strategies for Designing Photocaged Complexes for Zn2+ -- 9.4 Photocaged Complexes for Other Metal Ions -- 9.4.1 Photocaged Complexes for Copper -- 9.4.2 Photocaged Complexes for Iron -- 9.4.3 Photocaged Complexes for Other Metal Ions -- 9.5 Conclusions -- Acknowledgment -- References -- Chapter 10 Release of Bioactive Molecules Using Metal Complexes -- 10.1 Introduction -- 10.2 Small-molecule Messengers -- 10.2.1 Biological Generation and Delivery of CO, NO, and H_2S -- 10.2.2 Metal-Nitrosyl Complexes for the Cellular Delivery of Nitric Oxide -- 10.2.3 CO-releasing Molecules (CORMs) -- 10.3 "Photouncaging'' of Neurotransmitters from Metal Complexes -- 10.3.1 "Caged'' Compounds -- 10.3.2 "Uncaging'' of Bioactive Molecules -- 10.4 Hypoxia Activated Cobalt Complexes -- 10.4.1 Bioreductive Activation of Cobalt Complexes -- 10.4.2 Hypoxia-activated Cobalt Prodrugs of DNA Alkylators -- 10.4.3 Hypoxia-activated Cobalt Prodrugs of MMP Inhibitors -- 10.5 Summary -- Acknowledgments -- References -- Chapter 11 Metal Complexes as Enzyme Inhibitors and Catalysts in Living Cells -- 11.1 Introduction -- 11.2 Metal-based Inhibitors: From Serendipity to Rational Design -- 11.2.1 Mimicking the Structure of Known Enzyme Binders -- 11.2.2 Coordinating Known Enzymatic Inhibitors to Metal Complexes -- 11.2.3 Exchanging Ligands to Inhibit Enzymes -- 11.2.4 Controlling Conformation by Metal Coordination.

11.2.5 Competing with Known Metallo-Enzymatic Processes.