Elsevier S & T

Globins and Other Nitric Oxide-Reactive Proteins, Part A

Poole, Robert K.

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Table of contents
  • Contentsv
  • Contributorsxv
  • Prefacexxiii
  • Volumes in Seriesxxv
  • Section I: Nitric Oxide: Chemical and Analytical Methods1
  • Chapter 1: Chemistry of Nitric Oxide and Related Species3
  • 1. Introduction4
  • 2. Chemistry of NO5
  • 2.1. Properties of the NO molecule5
  • 2.2. Reaction of NO with oxygen7
  • 3. Compounds Related to NO8
  • 3.1. Nitroxyl HNO8
  • 3.2. Reactions of HNO11
  • 4. Nitrous Acid, Nitrosation, and S-Nitrosothiols11
  • 5. Reactions of Peroxynitrite, ONOO-12
  • 6. Nitrogen Dioxide13
  • 7. Nitrosative Stress and Reactive Nitrogen Species14
  • 8. NO Complexes with Metal Centers14
  • 9. Mobilization of Metal Ions from Biological Sites by NO15
  • 10. Scavenging NO with Metal Complexes16
  • References16
  • Chapter 2: Delivery of Nitric Oxide for Analysis of the Function of Cytochrome c'21
  • 1. Introduction21
  • 2. Steady-State Titration and Addition of NO into Anaerobic Cytochrome c'22
  • 3. Stopped-Flow Analysis of NO Ferrous Cytochrome c' Formation28
  • References21
  • Chapter 3: The Preparation and Purification of NO Gas and the Use of NO Releasers: The Application o35
  • 1. Introduction36
  • 2. Supply of NO37
  • 2.1. NO from cylinders and lecture bottles37
  • 2.2. Generation of NO in the laboratory38
  • 2.3. Determination of NO concentration39
  • 3. NO Releasers40
  • 3.1. S-nitrosothiols40
  • 3.2. Metal nitrosyl complexes41
  • 3.3. NOR, NOC, and NONOate compounds41
  • 4. Applications to Nitrosative Stress44
  • 4.1. Cellular fate of NO2 and the level of nitrosative stress44
  • 4.2. Microbes and nitrosative stress45
  • References21
  • Chapter 4: The Chemistry of Peroxynitrite: Implications for Biological Activity49
  • 1. Introduction50
  • 2. Mechanism of Peroxynitrite Decomposition in Aqueous Solutions51
  • 3. Reactivity of Peroxynitrite52
  • 4. The Radical Model In Vivo54
  • 5. Nitration of Tyrosine55
  • 6. Summary57
  • Acknowledgments57
  • References21
  • Chapter 5: Nitric Oxide Selective Electrodes63
  • 1. Significance of NO in Life Science64
  • 2. Methods of NO Measurement in Physiology64
  • 3. Advantages of Electrochemical Sensors for Determination of NO65
  • 4. Principles of Determination of NO by Electrochemical Sensors65
  • 5. Fabrication of Electrodes for NO Determination66
  • 5.1. Clark-type NO electrodes66
  • 5.2. Modified carbon-fiber NO microelectrodes68
  • 5.3. Integrated NO microelectrodes69
  • 5.4. Other NO electrodes70
  • 6. Calibration of NO Electrodes71
  • 6.1. Calibration using an NO standard solution72
  • 6.2. Calibration based on decomposition of SNAP72
  • 6.3. Calibration based on chemical generation of NO73
  • 7. Characterization of NO Electrodes74
  • 7.1. Sensitivity and detection limit75
  • 7.2. Selectivity76
  • 7.3. Response time77
  • 7.4. Effect of temperature and pH on NO electrodes78
  • 8. Selected Applications of NO Electrodes78
  • 9. Concluding Remarks and Other Directions88
  • Acknowledgments88
  • References88
  • Chapter 6: NO, N2O, and O2 Reaction Kinetics: Scope and Limitations of the Clark Electrode97
  • 1. Introduction98
  • 2. Materials99
  • 3. The Clark Electrode Holder99
  • 4. Schematics of the Clark-Electrode Setup101
  • 5. Performance of the Apparatus103
  • 5.1. Determination of NO reduction activity of Nor103
  • 5.2. Determination of N2O reduction activity of N2OR106
  • 5.3. O2 measurements107
  • 6. Scope and Limitations of the Clark Electrode109
  • Acknowledgments21
  • References21
  • Chapter 7: Chemiluminescence Quantification of NO and Its Derivatives in Liquid Samples113
  • 1. Introduction114
  • 1.1. The myriad roles of NO114
  • 1.2. The chemistry of NO115
  • 1.3. The NO-ozone reaction and the chemiluminescence analyzer115
  • 2. Methods117
  • 2.1. Determination of NO-2 concentration in liquid samples117
  • 2.2. Determination of NO-2 , NO-3 , and S-nitrosothiol concentrations in liquid samples119
  • 2.3. Determination of SNO concentration in liquid samples121
  • 3. Applications124
  • 3.1. Measurement of nitrate/nitrite in cell supernatants124
  • 3.2. Measurement of SNO in murine macrophage cell lysates125
  • 4. Final Remarks125
  • Acknowledgments21
  • References126
  • Section II: Bacterial and Archaeal Hemoglobins129
  • Chapter 8: Interactions of NO with Hemoglobin: From Microbes to Man131
  • 1. Introduction132
  • 2. Microbes, Plants, and Invertebrates133
  • 2.1. FHbs134
  • 2.2. Monomeric Hbs136
  • 2.3. Truncated Hbs138
  • 3. Yeast and Fungi139
  • 3.1. FHbs139
  • 4. Plants140
  • 4.1. Lbs140
  • 4.2. nsHbs142
  • 5. Invertebrates146
  • 5.1. Nematode worms146
  • 5.2. AHb: Structural and biochemical properties146
  • 5.3. Physiological role and biochemical mechanism147
  • 6. Mammals and Birds149
  • 6.1. Tetrameric hemoglobins149
  • 6.2. Tetrameric Hb: Structural and biochemical properties150
  • 6.3. Tetrameric Hb: Physiological role and biochemical mechanisms153
  • 6.4. Tetrameric Hb micropopulations154
  • 6.5. Tetrameric Hb oxidation and Hb-SNO formation156
  • 7. Experimental Design157
  • 8. Concluding Remarks159
  • References
  • Chapter 9: A Survey of Methods for the Purification of Microbial Flavohemoglobins169
  • 1. Introduction170
  • 2. The "BC" Era of Flavohemoglobin Purification and Characterization178
  • 2.1. An overview of recent methods for flavohemoglobin expression and purification178
  • 3. Methods for Expression and Purification of E. coli HMP179
  • 3.1. Expression and purification of E. coli HMP in pBR322, a multicopy vector179
  • 3.2. Expression and purification of E. coli HMP from the vector pPL452 and thermal induction180
  • 3.3. Expression of E. coli hmp in pBAD181
  • Acknowledgments
  • References182
  • Chapter 10: Structural Studies on Flavohemoglobins187
  • 1. Introduction188
  • 2. X-ray Structure of A. Eutrophus Flavohemoglobin189
  • 2.1. Crystallization189
  • 2.2. Data collection, data analysis, and structure solution189
  • 2.3. Model building and refinement191
  • 2.4. Lipid analysis191
  • 3. X-ray Structure of E. Coli Flavohemoglobin192
  • 3.1. Crystallization192
  • 3.2. Data collection, analysis, and structure solution192
  • 3.3. Model building and refinement193
  • 4. Structural Comparison Between A. Euthrophus and E. coli Flavohemoglobins193
  • 4.1. Overall fold193
  • 4.2. FAD-binding domain194
  • 4.3. NAD-binding domain196
  • 4.4. Heme-binding domain197
  • Acknowledgments201
  • References201
  • Chapter 11: Flavohemoglobin of Staphylococcus aureus203
  • 1. Introduction204
  • 2. Preparation of Recombinant S. aureus HMP204
  • 2.1. Protein expression205
  • 2.2. Protein purification205
  • 2.3. Physicochemical properties of S. aureus HMP206
  • 2.4. Redox titration and analysis206
  • 2.5. Catalytic properties of S. aureus HMP208
  • 3. Nitrosative Protection of S. aureus by HMP209
  • 3.1. RNA extraction and RT-PCR analysis209
  • 3.2. Construction of S. aureus hmp deletion strain209
  • 3.3. Protection of S. aureus by Hmp in response to GSNO and NO211
  • 3.4. Complementation analysis211
  • 4. Discussion212
  • Acknowledgments
  • References
  • Chapter 12: Assay and Characterization of the NO Dioxygenase Activity of Flavohemoglobins217
  • 1. Introduction218
  • 2. The bullNO Dioxygenase Mechanism218
  • 3. Susceptibility of the bullNO Dioxygenase to bullNO Inhibition219
  • 4. Autooxidation of Hemoglobins and bullNO Decomposition222
  • 5. Methemoglobin Reduction223
  • 6. Heme and Flavin Cofactors224
  • 7. bullNO Dioxygenase Assays225
  • 7.1. Reagents225
  • 8. Preparation of bullNO-, CO-, and O2- Saturated Solutions229
  • 8.1. Reagents and materials229
  • 9. Assay of Heme and FAD Content232
  • 9.1. Reagents232
  • 10. Reconstitution of Flavohemoglobin with Heme233
  • 10.1. Reagents233
  • 11. Assay for Nitrate and Nitrite Reaction Products234
  • 11.1. Reagents234
  • 12. Conclusions235
  • Acknowledgments
  • References
  • Chapter 13: Globin Interactions with Lipids and Membranes239
  • 1. Introduction240
  • 2. Lipid Extraction241
  • 2.1. Overview241
  • 2.2. Extraction method241
  • 3. Qualitative Analysis of Total Lipid Extracts242
  • 3.1. Overview242
  • 3.2. Transesterification reaction and GC/MS analysis242
  • 4. Hemoglobin-Liposome Binding Studies242
  • 4.1. Overview242
  • 4.2. Liposome preparations243
  • 4.3. Gel-filtration experiments243
  • 5. Lipid Monolayers as Models for Globin-Membrane Interaction Studies245
  • 5.1. Overview245
  • 5.2. Interaction of VHb with E. coli lipid monolayer246
  • 6. Lipid Binding Measurement by Absorption Spectroscopy248
  • 6.1. Overview248
  • 6.2. Lipid binding to VHb and HMP248
  • 7. Conclusions
  • Acknowledgments
  • References252
  • Chapter 14: Assessment of Biotechnologically Relevant Characteristics of Heterologous Hemoglobins in255
  • 1. Introduction256
  • 2. Expression Strategy260
  • 2.1. Gene placement and plasmid copy number260
  • 2.2. Transcriptional regulation261
  • 3. Considerations for the Choice of Growth Medium262
  • 3.1. Overview262
  • 4. Cofactor Imitation263
  • 5. Microaerobic Fed-Batch Cultivations264
  • 5.1. Overview264
  • 5.2. Small-scale bioreactor cultivations (300 ml)265
  • 5.3. Laboratory-scale bioreactor cultivations (1.3 l)266
  • 6. Physiological Analysis267
  • 6.1. DO, growth, carbon dioxide production, and oxygen uptake267
  • 6.2. By-product formation268
  • 7. Verification of Expression of Globin Proteins269
  • 7.1. CO-difference spectrum269
  • 7.2. Western blotting269
  • References270
  • Chapter 15: Applications of the VHB Gene VHB for Improved Microbial Fermentation Processes273
  • 1. Introduction274
  • 2. VHB Application in Microbial Metabolic Engineering275
  • 3. Effect of VHB on Protein Production276
  • 4. Effect of VHB on Polyhydroxyalkanoate Production279
  • 5. Effect of VHB on Antibiotic Production281
  • 6. Application of VHB in Bioremediation281
  • 7. Application of VGB Promoter282
  • 8. Future Prospects283
  • References
  • Chapter 16: Expression and Purification of CGB and CTB, the NO-Inducible Globins of the Foodborne B289
  • 1. Introduction290
  • 2. Methods for Cloning, Expression, and Purification of CGB293
  • 2.1. Cloning and expression of C. jejuni Cgb in E. coli293
  • 2.2. Purification of Cgb294
  • 2.3. Histidine-tagged Cgb: A cautionary note295
  • 3. Methods for Cloning, Expression, and Purification of CTB296
  • 3.1. Cloning and expression of C. jejuni trHB in E. coli296
  • 3.2. Purification of C. jejuni trHb298
  • 3.3. Visible absorbance spectroscopy298
  • Acknowledgments300
  • References300
  • Chapter 17: Mapping Heme-Ligand Tunnels in Group I Truncated(2/2) Hemoglobins303
  • 1. Introduction304
  • 2. The 2/2 Hemoglobin Fold305
  • 3. Protein Cavities/Tunnel and Ligand Entry306
  • 4. Experimental Procedures308
  • 4.1. Use of atomic coordinates to unravel protein matrix tunnels308
  • 4.2. The use of Xe atoms to map cavities in 2/2HBN308
  • 4.3. n-Butyl-isocyanide310
  • 5. Results310
  • 5.1. Mapping of protein matrix tunnels in 2/2HbN310
  • 5.2. 2/2HbN-Xe derivatives311
  • 5.3. 2/2HbN butyl-isocyanide derivatives312
  • 6. Conclusions312
  • Acknowledgments
  • References
  • Chapter 18: Scavenging of Reactive Nitrogen Species by Mycobacterial Truncated Hemoglobins317
  • 1. Introduction318
  • 2. Materials319
  • 2.1. Mycobacterial trHbs319
  • 2.2. Chemicals320
  • 3. bullNO Scavenging by M. tuberculosis trHbN(II)-O2 and trHbO(II)-O2 and by M. Leprae trHBO(II)-O2321
  • 3.1. Overview321
  • 3.2. Assay protocol324
  • 4. Peroxynitrite Scavenging by M. Leprae trHBO(II)-O2326
  • 4.1. Overview326
  • 4.2. Assay protocol328
  • 5. Peroxynitrite Scavenging by M. Leprae trHBO(II)-NO329
  • 5.1. Overview329
  • 5.2. Assay protocol331
  • 6. Structural Background331
  • Acknowledgments
  • References
  • Section III: Other Hemoglobins339
  • Chapter 19: Expression, Purification, and Crystallization of Neuro-and Cytoglobin341
  • 1. Introduction342
  • 2. Expression and Preparative Purification of Human Wild-Type NGB343
  • 2.1. Cloning of NGB cDNA in the expression vector343
  • 2.2. Expression of NGB343
  • 2.3. Preparative purification of recombinant Ngb344
  • 3. Expression and Preparative Purification of Human Wild-Type CYGB347
  • 3.1. Cloning of CYGB cDNA in the expression vector and expression of CYGB347
  • 3.2. Preparative purification of recombinant CYGB347
  • 4. Alternative Methods for the Preparative Purification of Recombinant NGB and CYGB and their Mutant349
  • 5. Analytical Purification of Recombinant Ngb and CYGB350
  • 5.1. Gel filtration on Superose 12 column: Separation of aggregates351
  • 5.2. Anion-exchange chromatography on a HiTrap DEAE fast-flow column353
  • 6. Crystallization of NGB and CYGB355
  • 6.1. Human NGB355
  • 6.2. Human CYGB356
  • Acknowledgments
  • References
  • Chapter 20: Measurement of Distal Histidine Coordination Equilibrium and Kinetics in Hexacoordinate359
  • 1. Introduction360
  • 2. Ligand Binding to HX361
  • 3. Reactions in the Ferrous Oxidation State363
  • 3.1. Methods363
  • 3.2. Analysis364
  • 4. Reactions in the Ferric Oxidation State367
  • 4.1. Methods367
  • 4.2. Analysis369
  • 5. Measurement of KH in the Ferrous Oxidation State Using Absorbance Spectroscopy370
  • 6. Measurement of KH by Electrochemistry371
  • 7. Conclusions376
  • References
  • Chapter 21: Purification of Class 1 Plant Hemoglobins and Examination of Their Functional Properties379
  • 1. Introduction380
  • 2. Purification of Barley Hemoglobin380
  • 2.1. Cloning barley hemoglobin in E. coli381
  • 2.2. Extraction and purification of recombinant barley Hb381
  • 2.3. Purification protocol382
  • 2.4. Molecular mass of recombinant Hb383
  • 2.5. Characterization of barley Hb383
  • 3. Measurement of NO Scavenging Activity384
  • 4. Identification of a Methemoglobin Reductase386
  • 4.1. Purification protocol for MDHA reductase387
  • 5. Conclusion389
  • References
  • Chapter 22: Use of In Silico (Computer) Methods to Predict and Anazlyze the Tertiary Structure of Pl393
  • 1. Introduction394
  • 1.1. Overview394
  • 1.2. Reported amino acid sequences and tertiary structures for plant hemoglobins401
  • 2. An In Silico Method for Predicting the Tertiary Structure of Rice HB2401
  • 3. Image Editing to Generate High-Quality Figures406
  • 3.1. Editing of helices and loops408
  • 3.2. Editing of the amino acid residues at the heme pocket408
  • Acknowledgments
  • References
  • Chapter 23: A Self-Induction Method to Produce High Quantities of Recombinant Functional Flavo-Legh411
  • 1. Introduction412
  • 2. A Self-Induction System for Overexpression of FLBR2414
  • 2.1. Medium growth and incubating conditions of the recombinant cells414
  • 2.2. Harvest and breaking of the E. coli cells415
  • 2.3. Purification of recombinant FLbR2415
  • 3. Spectroscopic Methods416
  • 3.1. UV-Visible spectra416
  • 3.2. Assays for the catalysis of Lb3+ reduction416
  • 4. Results417
  • 4.1. Representative purification and protein production yield417
  • 4.2. Purification of rFLbR-2: Purification assessment418
  • 4.3. UV-Vis spectra of the flavoenzyme418
  • 4.4. Functionality of the recombinant rFLbR-2420
  • 5. Conclusions421
  • Acknowledgments
  • References422
  • Chapter 24: Spectroscopic and Crystallographic Characterization of Bis-Histidyl Adducts in Tetramer425
  • 1. Introduction426
  • 2. Antarctic Fish Hemoglobins427
  • 3. Overview of the Combined Spectroscopic/Crystallographic Approach to the Characterization of Hemic428
  • 4. Hemichrome Formation and Detection429
  • 4.1. Hemichrome occurrence in Hbs429
  • 4.2. The exceptional behavior of Antarctic fish Hbs430
  • 4.3. Spectroscopic markers431
  • 5. Structural Characterization of Hemichrome in Tetrameric HBS434
  • 5.1. Crystallization434
  • 5.2. The available three-dimensional structural models435
  • 5.3. Atomic resolution structure of HbTb in partial hemichrome state438
  • 6. Conclusions440
  • Acknowledgments440
  • References440
  • Chapter 25: Dinitrosyl Iron Complexes Bind with Hemoglobin as Markers of Oxidative Stress445
  • 1. Introduction446
  • 1.1. Materials447
  • 1.2. Synthesis of DNIC447
  • 1.3. EPR assay448
  • 1.4. Experiments on animals448
  • 2. Formation of HB-DNIC In Vivo449
  • 2.1. Overview449
  • 2.2. Spin adducts of DEPMPO with free radicals449
  • 3. Influence of Hb-DNIC on Free Radical Generation During HB'S Interaction with Tert-Butyl Hydropero451
  • 4. Study of Oxidative HB Modification by SDS Electrophoresis451
  • 5. Influence of HB-DNIC on Oxidative Modification of HB Under the Action of Hydrogen Peroxide452
  • 5.1. Study of Hb-DNIC destruction by hydroperoxides453
  • 6. Influence of Tert-Butyl Hydroperoxide and Hydrogen Peroxide on HB-DNIC454
  • 6.1. Interaction between superoxide and HB-DNIC456
  • 7. Superoxide-Dependent Destruction of HB-DNIC456
  • 8. Conclusion459
  • Acknowledgments
  • References
  • Chapter 26: Linked Analysis of Large Cooperative, Allosteric Systems: The Case of the Giant HBL Hemo463
  • 1. Introduction464
  • 2. Materials466
  • 2.1. Hb preparation and oxygen-binding curves466
  • 3. Theory466
  • 3.1. Fitting function466
  • 3.2. Models466
  • 3.3. Influence of allosteric effectors469
  • 3.4. Constraints on the allosteric equilibrium constants471
  • 3.5. Statistics472
  • 4. HBL Hb from L. terrestris473
  • 5. HBL Hb from M. decora476
  • 6. What Is the Advantage of Hierarchical Function?478
  • 7. Concluding Remarks480
  • Appendix A481
  • References
  • Chapter 27: Mass Mapping of Large Globin Complexes by Scanning Transmission Electron Microscopy487
  • 1. Introduction488
  • 2. Description of STEM Mass Mapping488
  • 3. Advantages of STEM490
  • 4. STEM Specimen Preparation492
  • 5. Limitations of STEM493
  • 5.1. Molecular mass493
  • 5.2. Purity494
  • 5.3. Concentration494
  • 5.4. Buffers and salts494
  • 5.5. Stability of sample and denaturation495
  • 5.6. Substrate495
  • 6. STEM Operation496
  • 7. Interactive Mass Mapping with PCMass496
  • 8. Performance Checks498
  • 9. Applications499
  • References
  • Chapter 28: Mini-Hemoglobins from Nemertean Worms503
  • 1. Background503
  • 2. Isolation and Purification of C. lacteus HB504
  • 2.1. Anesthesia504
  • 2.2. Tissue Hb isolation505
  • 2.3. Tissue Hb purification506
  • 3. Other Nemertean HBS507
  • 3.1. Red Blood Cells507
  • 3.2. Collecting Nemerteans508
  • References
  • Chapter 29: Comparative and Evolutionary Genomics of Globin Genes in Fish511
  • 1. Introduction512
  • 2. Comparative Genomics of Fish Globin Genes513
  • 2.1. Available data sets513
  • 2.2. Bioinformatic tools for comparative genomics516
  • 2.3. Identifying orthologous and paralogous genes516
  • 2.4. Data set production517
  • 2.5. Performing multiple alignment518
  • 2.6. Phylogenetic analysis518
  • 2.7. Evaluating alternative phylogenetic hypotheses520
  • 3. Evolution of Globins and Identification of Functionally Relevant Amino Acid Residues520
  • 3.1. Type of selection acting on codons/amino acid residues520
  • 3.2. Detecting functionally diverging amino acid residues521
  • 3.3. Inferring ancestral globin sequences522
  • 3.4. General remarks523
  • 4. An Example of Comparative Genomics in Fish Globins523
  • 5. Cytogenetic Methods for Comparative Genomics: Fluorescence In Situ Hybridization526
  • 5.1. Mapping of globin genes by FISH on fish527
  • 5.2. The FISH procedure528
  • 5.3. General remarks531
  • References532
  • Chapter 30: Inferring Evolution of Fish Proteins: The Globin Case Study539
  • 1. Introduction540
  • 2. HB Purification542
  • 2.1. Hemolysate preparation542
  • 2.2. Hb separation542
  • 3. Elucidation of Globin Primary Structure542
  • 3.1. Globin separation542
  • 3.2. Modification of alpha and beta chains of fish hemoglobins543
  • 3.3. Protein cleavage543
  • 3.4. Deacylation of alpha-chain N terminus544
  • 4. Globin Characterization545
  • 4.1. Amino acid sequencing545
  • 4.2. Cloning and sequencing of globin cDNAs545
  • 5. Sequence Analysis546
  • 5.1. Homologous and paralogous copies546
  • 5.2. Sequence search in the databases546
  • 5.3. Sequence alignment547
  • 6. Phylogenetic Analysis548
  • 6.1. Overview of tree-building methods and topology interpretation548
  • 6.2. Approaching the species tree551
  • 6.3. Some reference species trees for Actinopterygians552
  • 6.4. Reconstruction of the history of a gene family553
  • 6.5. Reciprocal illumination555
  • 6.6. Reconstruction of character states at the nodes557
  • 6.7. Alternative reconstructions and interpretations557
  • 6.8. Adaptations and disadaptations558
  • 7. Bringing Phylogenetics and Structural Analysis Together559
  • 7.1. Identification of structural motifs559
  • 7.2. Molecular modeling560
  • 7.3. Functional divergence561
  • 8. General Remarks564
  • Acknowledgments
  • References
  • Chapter 31: Tracing Globin Phylogeny Using PSIBLAST Searches Based on Groups of Sequences571
  • 1. Introduction572
  • 2. Statistical Evaluation of Sequence Similarity573
  • 3. Verification of Globin Sequence Alignments574
  • 4. A New Paradigm in Globin Classification575
  • 5. Tracing Phylogenetic Relationships Via PSIBLAST Searches576
  • References
  • Author Index585
  • Subject Index615
Book details
  • Vendor Elsevier S & T
  • SKU 9780123742773
  • ISBN-13 9780080560441
  • Author Poole, Robert K.
  • Category Science
  • Subject Biochemistry

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This volume features methods for the study of globin and other nitric oxide-reactive proteins.