Biological inorganic chemistry: An introduction

Biological Inorganic Chemistry: An Introduction

Volumn , Issue , 2007, Pages 1-369

  Crichton, Robert R ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85135249794     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-444-52740-0.X5024-8     Document Type: Book

References (240)

1. Ash D.E. Arginine metabolism: enzymology, nutrition and clinical significance. J. Nutr. 2004, 134:2760S-2764S.
2. Barynin V.V., Whittaker M.M., Antonyuk S.V., Lamzin V.S., Harrison P.M., Artymiuk P.J., WhiMaker J.W. Crystal structure of manganese catalase from Lactobacillus plantarum. Structure 2001, 9:725-738.
3. Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S. Architecture of the pho- tosynthetic oxygen-evolving center. Science 2004, 303:1831-1838.
4. Goussias C., Boussac A., Rutherford A.W. Photosystem II and photosynthetic oxidation of water: an overview. Phil. Trans. R. Soc. Lond. B 2002, 357:1369-1381.
5. Iverson T.M. Evolution and unique bioenergetic mechanisms in oxygenic photosynthesis. Curr. Opin. Chem. Biol. 2006, 10:91-100.
6. Kok B., Forbush B., McGloin M.P. Cooperation of changes in photosynthetic Oinf2/inf-evolution-I: a linear four-step mechanism. Photochem. Photobiol. 1970, 11:457-475.
7. Loll B., Kern J., Saenger W., Zouni A., Biesiadka J. Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 2005, 438:1040-1044.
8. Miller A.-F. Superoxide dismutases: active sites that save, but a protein that kills. Curr. Opin. Chem. Biol. 2004, 8:162-168.
9. Rutherford A.W., Boussac A. Water photolysis in biology. Science 2004, 303:1782-1784.
10. Voet D., Voet J.G. Biochemistry 2004, Wiley, Hoboken, NJ, 1591 pp. 3rd edition.
11. Yocum C.F., Pecoraro V.L. Recent advances in the understanding of the biological chemistry of manganese. Curr. Opin. Chem. Biol. 1999, 3:182-187.
12. Barney B.M., Lukoyanov D., Yang T.-C., Dean D.R., Hoffman B.M., Seefeldt L.C. A metiiyldiazene (NH = N-CHinf3/inf)-derived species bound to the nitrogenase active-site FeMo cofactor: implications for mechanism. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:17113-17118.
13. Brondino C.D., Romao M.J., Moura I., Moura J.J.G. Molybdenum and tungsten enzymes: the xanthine oxidase family. Curr. Opin. Chem. Biol. 2006, 10:109-114.
14. Chatt J., Dilwordi J.R., Richards R.L. Recent advances in the chemistry of nitrogen fixation. Chem. Rev. 1978, 78:589-625.
15. Crans D.C., Smee J.J., Gaidamauskas E., Yang L. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chem. Rev. 2004, 104:849-902.
16. Downie J.A. Legume haemoglobins: symbiotic nitrogen fixation needs bloody nodules. Curr. Biol. 2005, 15:R196-R198.
17. Enemark J.H., Cooney J.J.A., Wang J.-J., Holm R.H. Synthetic analogues and reaction systems relevant to the molybdenum and tungsten oxotransferases. Chem. Rev. 2004, 104:1175-1200.
18. Hidai M. Chemical nitrogen fixation by molybdenum and tungsten complexes. Coord. Chem. Rev. 1999, 185 186:99 108.
19. Hille R. Molybdenum and tangsten in biology. TIBS 2002, 27:360-367.
20. Hille R. Molybdenum-containing hydroxylases. Arch. Biochem. Biophys. 2005, 433:107-116.
21. Howard J.B., Rees D.C. How many metals does it take to fix Ninf2/inf A mechanistic overview of biological nitrogen fixation. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:17088-17093.
22. Knowles J.R. Enzyme catalysis: not different, just better. Nature 1991, 350:121-124.
23. Ligtenbarg A.G.J., Hage R., Feringa B.L. Catalytic oxidations by vanadium complexes. Coord. Chem. Rev. 2003, 237:87-101.
24. Mayer S.M., Lawson D.M., Gormal C.A., Roe S.M., Smith B.E. New insights into structure-function relationships in nitrogenase: A 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein. J. Mol Biol. 1999, 292:871-891.
25. Mendel R.R., Bittner F. Cell biology of molybdenum. Biochim. Biophys. Acta 2006, 1763:621-635.
26. Nielsen F. Controversial chromium: does the superstar mineral of the mountebanks receive appropriate attention from clinicians and nutritionists?. Nutr. Today 1996, 31:226-233.
27. Ohshiro T., Littlechild J., Garcia-Rodriguez E., Isupov M.N., Iida Y., Kobayashi T., Izumi Y. Modification of halogen specificity of a vanadium-dependent bromoperoxidase. Protein Sci. 2004, 13:1566-1571.
28. Peters J.W., Szilagyi R.K. Exploring new frontiers of nitrogenase structure and function. Curr. Opin. Chem. Biol. 2006, 10:101-108.
29. Rees D.C, Tezcan F.A., Haynes C.A., Walton M.Y., Andrade S., Einsle O., Howard J.B. Structural basis of biological nitrogen fixation. Phil. Trans. R. Soc. 2005, 363:971-984.
30. Schrock R.R. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Acc. Chem. Res. 2005, 38:955-962.
31. Vincent J.B. The biochemistry of chromium. J. Nutr. 2000, 130:715-718.
32. Vincent J.B. Elucidating a biological role for chromium at a molecular level. Acc. Chem. Res. 2000, 33:503-510.
33. Vincent J.B. The potential value and potential toxicity of chromium picolinate as a nutritional supplement, weight-loss agent and muscle development agent. Sports Med. 2003, 33:213-230.
34. Vincent J.B. Recent advances in the nutritional biochemistry of trivalent chromium. Proc. Nutr. Soc. 2004, 63:41-47.
35. Yandulov D.V., Schrock R.R. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Science 2003, 301:76-78.
36. Barzilai A., Melamed E. Molecular mechanisms of selective dopaminergic neuronal death in Parkinson's disease. Trends Mol. Med. 2003, 9:126-132.
37. Bush A.I. The metallobiology of Alzheimer's disease. Trends Neurosci. 2003, 26:207-214.
38. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, Wiley, Chichester, 326 pp.
39. Crichton R.R., Ward R.J. Metal Based Neurodegeneration: From Molecular Mechanisms to Therapeutic Strategies 2006, Wiley, Chichester, 227 pp.
40. Curtain C.C., Ali F., Volitakis I., Cherny R.A., et al. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 2001, 276:20466-20473.
41. Dalle-Donne I., Giustarini D., Colombo R., Rossi R., Milzani A. Protein carbonylation in human diseases. Trends Mol. Med. 2003, 9:164-176.
42. Deisseroth K., Mermelstein P.G., Xia H., Tsien R.W. Signalling from synapse to nucleus: the logic behind the mechanisms. Curr. Opin. Neurobiol. 2003, 13:354-365.
43. Dürr A. Friedreich's ataxia: treatment within reach. Lancet Neurol 2002, 1:370-374.
44. Götz, M., Double K., Gerlach M., Youdim M.B.H., Riederer P. The relevance of iron in the pathogenesis of Parkinson's disease. Ann. N. Y. Acad. Sci. 2004, 1012:193-208.
45. Rogers J.T., Randall J.D., Cahill C.M., Eder P.S., et al. An iron-responsive element type II in the 5-untranslated region of the Alzheimers amyloid precursor protein transcript. J. Biol. Chem. 2002, 277:45518-45528.
46. Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10:S10-S17.
47. Voet D., Voet J.G. Biochemistry 2004, Wiley, Hoboken, NJ, 1591 pp. 3rd edition.
48. Wilquet V., De Strooper B. Amyloid-beta precursor protein processing in neurodegeneration. Curr. Opin. Neurobiol. 2004, 14:582-588.
49. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, 326. John Wiley Sons, Chichester.
50. Kauko A., Pullianen A.T., Haataja S., Mayer-Klauke W., Finne J., Papageorghiou A.C. Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core. J. Mol. Biol. 2006, 364:97-109.
51. Lewin A., Moore G.R., Le Brun N.E. Formation of protein-coated iron minerals. Dalton Trans. 2005, 22:3579-3610.
52. Mann S., Webb J., Williams R.J.P. Biomineralization Chemical and Biochemical Perspectives 1989, VCH, Wienheim, 541 pp.
53. Matsunaga T., Okamura Y. Genes and proteins involved in bacterial magnetic particle formation. Trends Microbiol. 2003, 11:536-541.
54. Nyraan J.S., Reyes M., Wang X. Effect of ultrastructural changes on the toughness of bone. Micron 2005, 36:566-582.
55. Su M., Cavallo S., Stefanini S., Chiancone E., Chasteen N.D. The so-called Listeria inocua ferritin is a Dps protein. Iron incorporation, detoxification and DNA protection properties. Biochemistry 2005, 44:5572-5578.
56. Thompson D.W. On Growth and Form 1942, Cambridge University Press, Cambridge, 1116 pp.
57. Toussaint L., Bertrand L., Hue L., Crichton R.R., Declercq J.-P. High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J. Mol. Biol. 2006, 365:440-452.
58. Wilt F.H. Developmental biology meets materials science: morphogenesis of biomineralized structures. Dev. Biol. 2005, 280:15-25.
59. Brabec V., Kasparkova J. inf78/infPt Platinum-Based Drugs. Metallo-therapeutic Drugs and Metal-based Diagnostic Agents. The Use of Metals in Medicine 2005, John Wiley and Sons, Chichester, 489-506 pp. M. Gielen, E.R. Tiekink (Eds.).
60. Crichton R.R., Ward R.J. Metal based Neurodegeneration: From Molecular Mechanisms to Therapeutic Strategies 2005, John Wiley Sons, Chichester, 227 pp.
61. Dzik-Jurasz A.S.K. Molecular imaging in vivo: an introduction. Br. J. Radiol. 2003, 76:S98-S109.
62. Gielen M., Tiekink E.R. Metallotherapeutic Drugs and Metal-Based Diagnostic Agents. The Use of Metals in Medicine 2005, Wiley, Chichester, 598 pp.
63. Martelli A., Rousselet E., Dycke C., Bouron A., Moulis J.-M. Cadmium toxicity in animal cells by interference with essential metals. Biochimie 2006, 88:1807-1814.
64. Martin R.B. Aluminum: A Neurotoxic Product of Acid Rain. Acc. Chem.Res. 1994, 27:204-210.
65. Meade T.J., Taylor A.K., Bull S.R. New magnetic resonance contrast agents as biochemical reporters. Curr. Opin. Neurobiol. 2003, 13:597-602.
66. Reedijk J. New clues for platinum antitumor chemistry: kinetically controlled meta binding to DNA. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:3611-3616.
67. Sigel A., Sigel H. Metal ions and their complexes in medication. Metal Ions Biol. Syst. 2004, 41. 519 pp.
68. Dutzler R., Campbell E.B., MacKinnon R. Gating the selectivity filter in C1C chloride channels. Science 2003, 300:108-112.
69. Gouax E., MacKinnon R. Principles of selective ion transport in channels and pumps. Science 2005, 310:1461-1465.
70. Levi P. The Periodic Table 1985, Michael Joseph, London, 233 pp.
71. Sacks O. Memories of a Chemical Boyhood. Uncle Tungsten 2001, Picador, London, 337 pp.
72. Constable E.C. Metals and Ligand Reactivity 1996, 1-21. VCH, Weinheim, Chapter 1.
73. Cotton F.A., Wilkinson G. Advanced Inorganic Chemistry: A Comprehensive Text 1980, Chichester, Wiley, New York, 1396 pp. 4th edition.
74. Huheey J.E., Keiter E.A., Keiter R.L. Inorganic Chemistry: Principles of Structure and Reactivity 1993, HarperCollins College Publishers, New York, 964 pp. 4th edition.
75. Mackay K.M., Mackay R.A. Introduction to Modern Inorganic Chemistry 1989, Blackie, Glasgow and London, 402 pp. 4th edition.
76. Al-Karadaghi S., Franco R., Hansson M., Shelnutt J.A., Isaya G., Ferreira G.C. Chelatases: distort to select?. TIBS 2006, 31:135-142.
77. Culotta V.C., Yang M., O'Halloran T.V.O Activation of superoxide dismutases: putting the metal to the pedal. Biochim. Biophys. Acta 2006, 1763:747-758.
78. Lill R., Duftkiewitz R., Elsässer H.-R., Haüsmann A., Netz D.J.A., Pierik A.J., Stehling O., Urzika E., Muhlenhoff U. Mechanisms of iron-sulfur protein mattiration in mitochondria, cytosol and nucleus of eukaryotes. Biochim. Biophys. Acta 2006, 1763:652-667.
79. Lill R., Mühlenhoff U. Iron-sulfur protein biogenesis in eukaryotes. TIBS 2005, 30:133-141.
80. Lill R., Mühlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 2006, 22:457-486.
81. Lippard S.J., Berg J.M. Principles of Bioinorganic Chemistry 1994, University Science Books, Mill Valley, CA, 411 pp.
82. Mason A.B., Halbrooks P.J., James N.G., Connolly S.A., Larouche J.R., Smith V.C., MacGillivray R.T.A., Chasteen N.D. Mutational analysis of C-lobe ligands of human serum Transferrin: insights into the mechanism of iron release. Biochemistry 2005, 44:8013-8021.
83. Mendel R.R., Bittner F. Cell biology of molybdenum. Biochim. Biophys. Acta 2006, 1763:621-635.
84. Parkin A., Cavazza C., Fontecilla-Camps J.C., Armstrong F.C. Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulphovibrio desulfuricans. JACS 2006, 128:16808-16815.
85. Rao P.V., Holm R.H. Synthetic analogues of the active sites of iron-sulfur proteins. Chem. Rev. 2004, 104:527-559.
86. Rees D.C. Great metalloclusters in enzymology. Annu. Rev. Biochem. 2002, 71:221-246.
87. Voet D., Voet J.G. Biochemistry 2004, John Wiley Sons, Chichester. 3rd edition.
88. Abrahams K.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of Finf1/inf,-ATPase from bovine heart mitochondria. Nature 1994, 370:621-628.
89. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2002, W.H. Freeman and Co., New York, 974 pp. 5th edition.
90. Campbell P.N., Smith A.D., Peters T.J. Biochemistry Illustrated: Biochemistry and Molecular Biology in the Post-Genomic Era 2005, Elsevier, London and Oxford, 242 pp. 5th edition.
91. Capaldi R., Aggeler R. Mechanism of Finf1/inf,Finf0/inf-type ATP synthase, a biological rotary motor. TIBS 2002, 27:154-160.
92. Devlin T.M. Textbook of Biochemistry with Clinical Correlations 2005, Wiley, Hoboken,NJ, 1208 pp. 6th edition.
93. Knowles J.R. Enzyme catalysis: not different, just better. Nature 1991, 350:121-124.
94. Voet D., Voet J.G. Biochemistry 2004, Wiley, Hoboken, NJ, 1591 pp. 3rd edition.
95. Anfinen C.B. Principles that govern the folding of protein chains. Science 1973, 181:223-230.
96. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2002, W.H. Freeman and Co., New York, 974 pp. 5th edition.
97. Branden C., Tooze J. Introduction to Protein Structure 1991, Garland Publishing, Inc., New York and London, 302 pp.
98. Campbell P.N., Smith A.D., Peters T.J. Biochemistry Illustrated Biochemistry and Molecular Biology in the Post-Genomic Era 2005, Elsevier, London and Oxford, 242 pp. 5th edition.
99. Chapeville F., Lipmann F., von Ehrenstein G., Weisblum B., Ray W.J., Benzer S. On the role of soluble ribonucleic acid in coding for amino acids. Proc. Natl. Acad. Sci. U.S.A. 1962, 48:1086-1092.
100. Creighton T.E. Proteins Structures and Molecular Properties 1993, W.H. Freeman and Co., New York, 507 pp. 2nd edition.
101. Eisenberg D. The discovery of the helix and the sheet, the principal structural features of proteins. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:11207-11210.
102. Fersht, A. Structure and Mechanism in Protein Science: A guide to Enzyme Catalysis and Protein Folding 1999, W.H. Freeman and Co., New York, 631 pp.
103. Moore P.B., Steitz T.A. The ribosome revealed. TIBS 2005, 30:281-283.
104. Rodnina M.V., Beringer M., Wintermeyer W. How ribosomes make peptide bonds. TIBS 2007, 32:20-26.
105. Selmer M., Dunham C.M., Murphy F.V., Weixlbaumer A., Petry S., Kelley A.C., Weir J.R., Ramakrishnan V. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 2006, 313:1935-1943.
106. Voet D., Voet J.G. Biochemistry 2004, Wiley, Hoboken, NJ, 1591 pp. 3rd edition.
107. Watson J.D., Crick F.H.C. Genetical implications of the structure of deoxyribonucleic acid. Nature 1953, 171:964-967.
108. Yonath A. Ribosomal Crystallography: Peptide Bond Formation, Chaperone Assistance and Antibiotics Activity. Mol. Cells 2005, 20:1-16.
109. Yonath A., Leonard K.R., Wittmann H.G. A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction. Science 1987, 236:813-816.
110. Arnesano F., Banci L., Piccioli M. NMR structures of paramagnetic proteins. Q. Rev. Biopkys. 2005, 38:167-219.
111. Banci L., Bertini I., Cantini P., Felli I.C., Gonnelli L., Hadjiliadis N., Pierattelli R., Rosato A., Voulgaris P. The Atx 1-Ccc2 complex is a metal-mediated protein-protein interaction. Nat. Chem. Biol. 2006, 2:367-368.
112. Bertini I., Luchinat C., Parigi G., Pierattelli R. NMR spectroscopy of paramagnetic metalloproteins. Chembiochem 2005, 6:1536-1549.
113. Campbell I.D., Dwek R.A. Biological Spectroscopy 1984, Benjamin/Cummings Publishing Co., Inc., Menlo Park, CA, 404 p.
114. Cowan J.A. Inorganic Biochemistry An Introduction 1997, 73. Wiley-VCH, New York. 2nd edition.
115. Ealick S.E. Advances in multiple wavelength anomalous diffraction crystallography. Curr. Opin. Chem. Biol. 2000, 4:495-499.
116. Fragai M., Luchinat C., Parigi G. "Four-dimensional" protein structures: examples from metalloproteins. Ace. Chem. Res. 2006, 39:909-917.
117. Hagen W.R. EPR spectroscopy as a probe of metal centres in biological systems. Dalton Trans. 2006, 37:4415-4434.
118. Neese F. Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mössbauer properties. Curr. Opin. Chem. Biol. 2003, 7:125-135.
119. Que L. Physical Methods in Bioinorganic Chemistry: Spectroscopy and Magnetism 2000, 59-120. University Science Books, Sausalito, CA.
120. Ubbink M., Worrall J.A.R., Canters G.W., Groenen E.J.J., Huber R. Paramagnetic resonance of biological metal centers. Annu. Rev. Biophys. Biomol. Struct. 2002, 31:393-422.
121. Andrews N.C. Iron homeostasis: insights from genetics and animal models. Nat. Rev. Genet. 2000, 1:208-217.
122. Andrews S.C., Robinson A.K., Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol. Rev. 2003, 27:215-237.
123. Cobine P.A., Pierrel F., Winge D.R. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes, Biochim. Biophys. Acta 2006, 1763:759-772.
124. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, Wiley, Chichester, 326 pp.
125. Eide D.J. The SLC39 family of metal ion transporters. Pflügers Arch. Eur. J. Physiol. 2004, 447:796-800.
126. Eide D.J. Zinc transporters and the cellular trafficking of zinc. Biophys. Biochim. Acta 2006, 1763:711-722.
127. Hantke K. Bacterial zinc transporters and regulators. Biometals 2001, 14:139-249.
128. Kosman D.J. Molecular mechanisms of iron uptake in fungi. Molec. Microbiol. 2003, 47:1185-1197.
129. Kwok E.Y., Severance S., Kosman D.J. Evidence for iron channeling in the Fet3p-Ftrlp high-affinity iron uptake complex in the yeast plasma membrane. Biochemistry 2006, 45:6317-6327.
130. Palmiter R.D., Huang L. Efflux and compartmentalisation of zinc by members of the SLC30 family of solute carriers. Pflügers Arch. Eur. J. Physiol. 2004, 447:744-751.
131. Petris M.J. The SLC31 (Ctr) copper transporter family. Pflügers Arch. Eur. J. Physiol. 2004, 447:796-800.
132. Schmidt W. Iron solutions: acquisition strategies and signalling pathways in plants. Trends Plant Sci. 2003, 8:188-193.
133. Solioz M., Stoyanov J.V. Copper homeostasis in Enterococcus hirae. FEMS Microbiol. Rev. 2003, 27:183-195.
134. Ambrus A., Chen D., Dai J., Bialis T., Jones R.A., Yang D. Human telomeric sequence forms a hybrid-type intramolecular G-quadruplex structure with mixed parallel/antiparallel strands in potassium solution. Nucleic Acids Res. 2006, 34:2723-2735.
135. Corry B., Chung S.-H. Mechalisms of valence selectivity in biological ion channels. Cell Mol. Life Sci. 2006, 63:301-315.
136. Doyle D.A., Cabral J.M., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., MacKinnon R. The structure of the potassium channel: molecular basis of Ksup+/sup conduction and selectivity. Science 1998, 280:69-77.
137. Gouax E., MacKinnon R. Principles of selective ion transport in channels and pumps. Science 2005, 310:1461-1465.
138. Hodgkin A.L., Huxley A.F. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 1952, 117:500-544.
139. Li X., Liu Y., Alvarez B.V., Casey J.R., Fliegel L. A novel carbonic anhydrase II binding site regulates NHE1 activity. Biochemistry 2006, 45:2414-2424.
140. MacKinnon R. Potassium channels and the atomic basis of selective ion conduction (Nobel lecture). Angew. Chem. Int. Edn. 2004, 43:4265-4277.
141. Orlowski J., Grinstein S. Diversity of the mammalian sodium/proton exchanger SLC9 family. Pflugers Arch. Eur. J. Physiol. 2004, 447:549-565.
142. Voet D., Voet J.G. Biochemistry 2004, Wiley, Hoboken, NJ, 1591 pp. 3rd edition.
143. Wozki S.A., Schmidt F.J. DNA and RNA: composition and structure. Textbook of Biochemistry with Clinical Correlations 2002, 45-92. 5th edition. T.M. Devlin (Ed.).
144. Yu F.H., Yarov-Yarovoy V., Gutman G.A., Catterall W.A. Overview of molecular relationships in the voltage-gated ion channel superfamily. Pharmacol. Rev. 2005, 57:387-395.
145. Andrews S.C., Robinson A.K., Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol. Rev. 2003, 27:215-237.
146. Andrews S.C. Iron storage in bacteria. Adv. Microb. Physiol. 1998, 40:281-351.
147. Bertinato J., L'Abbé MR. Maintaining copper homeostasis: regulation of copper-trafficking proteins in response to copper deficiency or overload. J. Nutr. Biochem. 2004, 15:316-322.
148. Cobine P.A., Pierrel F., Winge DR. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochim. Biophys. Acta 2006, 1763:759-772.
149. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, Wiley, Chichester, 326 pp.
150. Eide D.J. Zinc transporters and the cellular trafficking of zinc. Biochim. Biophys. Acta 2006, 1763:711-722.
151. Grotz N., Guerinot M.L. Molecular aspects of Cu, Fe and Zn homeostasis in plants. Biochim. Biophys. Acta 2006, 1763:595-608.
152. Hantke K. Bacterial zinc transporters and regulators. BioMetals 2001, 14:139-249.
153. Hantke K. Bacterial zinc uptake and regulators. Curr. Opin. Microbiol. 2005, 8:196-202.
154. Hell R., Stephan U.W. Iron uptake, trafficking and homeostasis in plants. Planta 2003, 216:541-551.
155. MacGillivray R.T., Moore S.A., Chen J., Anderson B.F., Baker H., Luo Y., Bewley M., Smith C.A., Murphy M.E., Wang Y., Mason A.B., Woodworth R.C., Brayer G.D., Baker E.N. Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry 1998, 37:7919-7928.
156. Magnani D., Solioz M. Copper chaperone cycling and degradation in the regulation of the cop operon of Enterococcus hirae. BioMetals 2005, 18:407-412.
157. Massé E., Gottesman S. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci., U.S.A. 2002, 99:4620-4625.
158. Pohl E., Haller J.C., Mijovilovich A., Meyer-Klauke W., Garman E., Vasil M.L. Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Molec. Microbiol. 2003, 47:903-915.
159. Rutherford J.C., Bird A.J. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell 2004, 3:1-13.
160. Schmidt W. Iron solutions: acquisition strategies and signaling pathways in plants. TIBS 2003, 8:188-193.
161. Vaulont S., Lou D.-Q., Viatte L., Kahn A. Of mice and men: the iron age. J. Clin. Invest. 2005, 115:2079-2082.
162. Wallander M.L., Leibold E.A., Eisenstein R.S. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta 2006, 1763:668-689.
163. Allen K.N., Dunaway-Mariano D. Phosphoryl group transfer: evolution of a catalytic scaffold. TIBS 2004, 29:495-503.
164. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2001, Freeman, New York, 974 pp. 5th edition.
165. Cowan J.A. Structural and catalytic chemistry of magnesium-dependent enzymes. BioMetals 2002, 15:225-235.
166. Frausto da Silva J.J.R., Williams R.J.P. The biological chemistry of the elements 2nd edition 2001, 270. Oxford University Press, Oxford.
167. Gerlt J.A., Babbitt P.C., Rayment I. Divergent evolution in the enolase superfaraily: the interplay of mechanism and specificity. Arch. Biochem. Biophys. 2005, 433:59-70.
168. Grueninger D., Schultz G.E. Structure and reaction mechanism of L-rhamnulose kinase from Eschericia coli. J. Mol. Biol. 2006, 359:787-797.
169. Knowles J.R. Enzyme-catalysed phosphoryl transfer reactions. Annu. Rev. Biochem. 1980, 49:877-919.
170. Larsen T.M., Wedeking J.E., Rayment I., Reed G.H. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 Å resolution. Biochemistry 1996, 30:4349-4358.
171. Maguire M.E., Cowan J.A. Magnesium chemistry and biochemistry. BioMetals 2002, 15:203-210.
172. Nowotny M., Yang W. Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release. EMBO J. 2006, 25:1924-1933.
173. Peeraer Y., Rabijns A., Collet J.-F., Van Scaftingen E., De Ranter C. How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. Eur. J. Biochem. 2004, 271:3421-3427.
174. Pingoud A., Fuxreiter M., Pingoud V., Wende W. Type II restriction endonucleases: structure and mechanism. Cell.Mol.Life Sci. 2005, 62:685-707.
175. Steitz T.A., Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:6498-6502.
176. Voet D., Voet J.G. Biochemistry 2004, Wiley, New York, Chichester, 1591 pp. 3rd edition.
177. Yang W., Lee J.Y., Nowotny M. Making and breaking nucleic acids: two-Mgsup2+/sup-ion catalysis and substrate specificity. Mol. Cell 2006, 22:5-13.
178. Auld D.S. Zinc coordination sphere in biochemical zinc sites. BioMetals 2001, 14:271-313.
179. Klug A., Rhodes D. 'Zinc fingers': a novel protein motif for nucleic acid recognition. TIBS 1988, 12:464-469.
180. Lipscomb W.N., Sträter N. Recent advances in zinc enzymology. Chem. Rev. 1996, 96:2375-2433.
181. McCall K.A., Huang C.-C., Fierke C.A. Function and mechanism of zinc metalloenzymes. J. Nutr. 2000, 130:1437S-1446S.
182. Parkin G. Synthetic analogues relevant to the structure and function of zinc enzymes. Chem. Rev. 2004, 104:699-767.
183. Tanaka Hall T.M. Multiple modes of RNA recognition by zinc finger proteins. Curr. Opin. Struct. Biol. 2005, 15:367-373.
184. Voet D., Voet J.G. Biochemistry 2004, Wiley, New York, Chichester, 1360 pp. 3rd edition.
185. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2002, Freeman, New York, 974 pp. 5th edition.
186. Carafoli E. The calcium cycle of mitochondria. FEBS Letts. 1979, 104:1-5.
187. Carafoli E. Calcium signalling: a tale for all seasons. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:1115-1122.
188. Carafoli E. Historical review: mitochondria and calcium: ups and downs of an unusual relationship. Trends Biochem. Sci. 2003, 28:175-181.
189. Carafoli E. Calcium-mediated cellular signals: a story of failures. Trends Biochem. Sci. 2004, 29:371-379.
190. Carafoli E. Calcium-a universal carrier of biological signals. FEBS J. 2005, 272:1073-1089.
191. Guerini D., Coletto L., Carafoli E. Exporting calcium from cells. Cell Calcium 2005, 38:281-289.
192. Rizzuto R., Brini M., Murgai M., Pozzan T. Microdomains with high Casup2+/sup close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 1993, 262:744-747.
193. Voet D., Voet J.G. Biochemistry 2004, Wiley, New York, Chichester, 1591 pp. 3rd edition.
194. Williams R.J.P. The evolution of calcium biochemistry. Biochim. Biophys. Acta 2006, 1763:1139-1146.
195. Collman J.P., Boulatov R., Sunderland C.J., Fu L. Functional analogues of cytochrome c oxidase, myoglobin and hemoglobin. Chem. Rev. 2004, 104:561-588.
196. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, 326. Wiley, Chichester.
197. Crichton R.R., Pierre J.-L. Old iron, young copper: from Mars to Venus. Biometals 2001, 14:99-112.
198. Fenton H.J.H. Trans. Chem. Soc. 1894, 65:899-910.
199. Fontecave M., Atta M., Mulliez E. S-adenosylmethionine: nothing goes to waste. TIBS 2004, 29:243-249.
200. Gelin B.R., Karplus M. Mechanism of tertiary structural change in hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1977, 74:801-805.
201. Haber F., Weiss J. The catalytic decomposition of hydrogen peroxide by iron salts. Proc. Roy. Soc. Ser. A. 1934, 147:332-351.
202. Hunte C, Koepke J., Lange C., Rossmanith T., Michel H. Structure at 2.3 Å resolution of the cytochrome bcinf1/inf complex from the yeast Saccharomyces cerevisiae with an antibody Fv fragment. Structure 2000, 8:669-684.
203. Imlay J.A. Iron-sulphur clusters and the problems with oxygen. Mol. Microbiol. 2006, 59:1073-1082.
204. Iverson T.M., Luna-Chavez C, Croal L.R., Cecchini G., Rees D.C. Crystallographic studies of the Eschericia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J. Biol. Chem. 2002, Ill:16124-16130.
205. Koehntop K.D., Emerson J.P., Que L. The 2-His-l-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J. Biol. Inorg. Chem. 2005, 10:87-93.
206. Kolberg M., Strand K.R., Graff P., Andersson K.K. Structure, function and mechanism of ribonucleotide reductases. Biochim. Biophys. Acta 2004, 1699:1-34.
207. Mitchell P. Protonmotive redox mechanism of the cytochrome b-cinf1/inf complex in the respiratory chain: protonmotive ubiquinone cycle. FEBS Lett. 1975, 56:1-6.
208. Namslauer A., Brzezinski P. Structural elements involved in electron-coupled proton transfer in cytocrome c oxidase. FEBS Lett. 2004, 567:103-110.
209. Nordlund P., Eklund H. Di-iron-carboxylate proteins. Curr. Opin. Struct. Biol. 1995, 5:758-766.
210. Rao P.V., Holm R.H. Synthetic analogues of the active sites of iron-sulfur proteins. Chem. Rev. 2004, 104:527-559.
211. Rees D.C. Great inetalloclusters in enzymology. Annu. Rev. Biochem. 2002, 71:221-246.
212. Sazinsky M.H., Lippard S.J. Correlating structure with function in bacterial raulticom- ponent monooxygenases and related diiron proteins. Acc. Chem. Res. 2006, 39:558-566.
213. Stubbe J., Ge J., Yee C.S. The evolution of ribonucleotide reduction revisited. TIBS 2001, 26:93-99.
214. Voet D., Voet J.G. Biochemistry 2004, 1591. Wiley, Hoboken, NJ. 3rd edition.
215. Banerjee R., Ragsdale S.W. The many faces of vitamin Binf12/inf: catalysis by cobalamin-dependent enzymes. Annu. Rev. Biochem. 2003, 72:209-247.
216. Drennan C.L., Doukov T.I., Ragsdale S.W. The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures. J. Biol. Inorg. Chem. 2004, 9:511-515.
217. Hegg E.L. Unravelling the structure and mechanism of acetyl-coenzyme A synthase. Acc. Chem. Res. 2004, 37:775-783.
218. Kobayashi M., Shimizu S. Cobalt proteins. Eur. J. Biochem. 1999, 261:1-9.
219. Mulrooney S.B., Hausinger R.P. Nickel uptake and utilisation by microorganisms. FEMS Microbiol. Rev. 2003, 27:239-269.
220. Ragsdale S.W. Nickel biochemistry. Curr. Opin. Chem. Biol. 1998, 2208-2215.
221. Ragsdale S.W. Life with carbon monoxide. Crit. Rev. Biochem. Mol. Biol. 2004, 39:165-195.
222. Ragsdale S.W. Metals and their scaffolds to promote difficult enzymatic reactions. Chem. Rev. 2006, 106:3317-3337.
223. Shima S., Warkentin E., Thauer R.K., Ermler U. Structure and function of enzymes involved in the methanogenic pathway utilising carbon dioxide and molecular hydrogen. J. Biosci. Bioeng. 2002, 93:519-530.
224. Svetlitchnyi V., Dobbek H., Meyer-Klauke W., Meins T., Thiele B., Römer P., Huber R., Meyer O. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:446-451.
225. Bento I., Carrondo M.A., Lindley P.F. Reduction of dioxygen by enzymes containing copper. J. Biol. Inorg. Chem. 2006, 11:539-547.
226. Brunori M., Giuffrè A., Sarti P. Cytochrome c oxidase, ligands and electrons. J. Inorg. Biochem. 2005, 99:324-336.
227. Chen P., Gorelsky S.I., Ghosh S., Solomon E.I. Ninf2/infO reduction by the inf4/inf-sulfide-bridged tetranuclear CuinfZ/inf cluster active site. Angew. Chem. Int. Ed. 2004, 43:4132-4140.
228. Crichton R.R. Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences 2001, Wiley, Chichester, 326 pp.
229. Crichton R.R., Pierre J.-L. Old iron, young copper: from Mars to Venus. BioMetals 2001, 14:99-112.
230. Crichton R.R., Ward R.J. Metal-Based Neurodegeneration from Molecular Mechanisms to Therapeutic Strategies 2006, Wiley, Chichester, 227 pp.
231. Granata A., Monzani E., Casella L. Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complex. J. Biol. Inorg. Chem. 2004, 9:903-913.
232. Harris Z.L., Davis-Kaplan S.R., Gitlin J.D., Kaplan J. A fungal multicopper oxidase restores iron homeostasis in aceruloplasminemia. Blood 2004, 103:4672-4673.
233. Hart P.J. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr. Opin. Chem. Biol. 2006, 10:131-138.
234. Hatcher L.Q., Karlin K.D. Oxidant types in copper-dioxygen chemistry: the ligand coordination defines the Cuinfn/inf-Oinf2/inf structure and subsequent reactivity. J. Biol. Inorg. Chem. 2004, 9:669-683.
235. Hellman N.E., Gitlin J.D. Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 2002, 22:439-458.
236. Lieberman R.L., Rosenzweig A.C. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 2005, 434:177-182.
237. Handbook of Metalloproteins 2001, Wiley, Chichester, 227 pp. A. Messerschmidt, R. Huber, T. Poulos, K. Weighardt (Eds.).
238. Potter S.Z., Valentine J.S. The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). J. Biol. Inorg. Chem. 2003, 8:373-380.
239. Riva S. Laccases: blue enzymes for green chemistry. TIBS 2006, 24:219-226.
240. Vallee B.L., Williams R.J. Metalloenzymes: the entatic nature of their active sites. Proc. Natl. Acad. Sci. USA 1968, 59:498-505.