Iron Porphyrins

1. Magnetic Circular Dichroism Spectroscopy of Iron Porphyrins and Heme Proteins; John H. Dawson and David M. Dooly; A. Introduction; B. Simple Heme Proteins and Model Iron Heme Complexes; i. Hemoglobin and Myoglobin; ii. Leghemoglobin; iii. Tryptophan and Indoleamine Dioxygenases; iv. Cytochrome b and Hemopexin; v. Peroxidases; vi. Catalase; vii. Cytochromes c and f; viii. Cytochrome P--450; ix. Chloroperoxidase; x. Additional Iron Heme Model Complexes; C. Multiheme--Containing Enzymes; i. Mammalian Cytochrome c Oxidase; ii. Pseudomonas Cytochrome Oxidase (Cytochrome cd, Nitrite Reductase); Acknowledgments; Notes; References; Addendum to Chapter 1: Recent Advances in the Magnetic Circular Dichroism Spectroscopy of Iron Porphyrins and Heme Proteins; John H. Dawson and David M. Dooley; A. Introduction; B. Simple (Noninteracting) Heme Proteins and Model Iron Porphyrin Complexes; i. Hemoglobin, Myoglobin, and Leghemoglobin; ii. Indoleamine Dioxygenase, Prostaglandin H Synthase, and Cytochrome c-; iii. Cytochromes b 5 , b 562 , c, c 3 , and c 551 ; iv. Formate Dehydrogenase and Nitrate Reductase; v. Peroxidases; vi. Cytochrome P--450 and Chloroperoxidase; vii. Yeast Complex III; viii. Additional Heme Proteins and Models; C. Multiheme Enzymes; i. Introduction; ii. Mammalian Cytochrome c Oxidase; iii. Pseudomonas aeruginosa Cytochrome Oxidase (Cytochrome cd, Nitrite Reductase); iv. Pseudomonas aeruginosa Cytochrome c--551 Peroxidase; v. Wolinella succinogenes Nitrite Reductase; Acknowledgments; References; 2. Mossbauer Spectroscopy of Iron Porphyrins; P. G. Debrunner; A. Introduction; B. Formalism; C. Experimental Considerations; D. Low--Spin Ferric Complexes, S = 1/2; E. Ferric High Spin, S = 5/2; F. Ferric Intermediate Spin, S = 3/2; G. Ferrous Low Spin, S = 0; i. PFeLL'; ii. PFeLCO; iii. PFeLO 2 ; H. Ferrous High Spin, S = 2; I. Ferrous Intermediate Spin, S = 1; J. Ferryl Porphyrins and Other Higher Oxidation States; K. Miscellaneous Cases; i. Hemoglobin NO; ii. Spin Transitions; iii. Porphyrin Dimers; iv. Spin--Coupled Systems; L. Iron Phthalocyanine; M. Iron Porphyrin Literature to Mid 1987; Notes; References; 3. X--Ray Absorption Spectroscopy of Iron Porphyrins; James E. Penner--Hahn and Keith O. Hodgson; A. Introduction; B. Physical Principles of X--Ray Absorption; i. X--Ray Absorption Edge Structure; ii. EXAFS; iii. Strengths and limitations; C. Experimental Considerations; i. Sample Requirements; ii. Equipment and Data Collection Requirements; iii. Potential Problems; D. X--Ray Absorption Data Analysis; i. Data Reduction; ii. Techniques of Data Analysis; iii. Sources of Error; E. Applications of X--Ray Absorption Spectroscopy to Porphyrins; i. Model Compounds, EXAFS; ii. Model Compounds, XANES; iii. Hemoglobin and Myoglobin; iv. Electron Transfer Hemoproteins; v. Cytochrome P--450 and Chloroperoxidase; vi. Horseradish Peroxidase; vii. Cytochrome--c Oxidase; F. Future Developments and Applications; Acknowledgments; References; Index