Biological Inorganic Chemistry

Biological Inorganic Chemistry

Volumn , Issue , 2012, Pages

  Crichton, Robert ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85013896748     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/C2010-0-66405-4     Document Type: Book

References (392)

1. Bienert G.P., Schüssler M.D., Jahn T.P. Metalloids: essential, beneficial or toxic? Major intrinsic proteins sort it out. Trends in Biochemical Sciences 2008, 33:20-26.
2. Di Bona K.R., Love S., Rhodes N.R., McAdory D., Sinha S.H., Kern N., et al. Chromium is not an essential trace element for mammals: effects of a "low-chromium" diet. The Journal of Biological Inorganic Chemistry 2010, 16:381-390.
3. Gouaux E., MacKinnon R. Principles of selective ion transport in channels and pumps. Science 2005, 310:1461-1465.
4. Flohé L. The labour pains of biochemical selenology: the history of selenoprotein biosynthesis. Biochimica et Biophysica Acta 2009, 1790:1389-1403.
5. Levi P. The periodic table 1985, Michael Joseph, London, p. 233.
6. Sacks O. Uncle tungsten. Memories of a chemical boyhood 2001, Picador, London.
7. Takano J., Miwa K., Fujiwara T. Boron transport mechanisms: collaboration of channels and transporters. Trends in Plant Science 2008, 13:451-457.
8. Wolfe-Simon F., et al. A bacterium that can grow by using arsenic instead of phosphorus. Science 2010, 2 Dec, 2010.
9. Constable E.C. Metals and ligand reactivity 1996, Chapter 1, VCH Weinheim, pp. 1-21.
10. Cotton F.A., Wilkinson G. Advanced inorganic chemistry: A comprehensive text 1980, John Wiley and Sons, New York, Chichester, pp. 1396. 4th ed.
11. Huheey J.E., Keiter E.A., Keiter R.L. Inorganic chemistry: Principles of structure and reactivity 1993, Benjamin Cummings. 4th ed.
12. Kirchner B., Wennmohs F., Ye S., Neese F. Theoretical bioinorganic chemistry: the electronic structure makes a difference. Current Opinion in Chemical Biology 2007, 11:134-141.
13. Mackay K.M., Mackay R.A. Introduction to modern inorganic chemistry 1989, Blackie, Glasgow and London, pp. 402. 4th ed.
14. Neese F. Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mössbauer properties. Current Opinion in Chemical Biology 2003, 7:125-135.
15. Anfinsen C.B. Principles that govern the folding of protein chains. Science 1973, 181:223-230.
16. Branden C., Tooze J. Introduction to protein structure 1991, Garland Publishing, Inc, New York and London, 302.
17. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2002, W.H. Freeman and Co, New York, 974. 5th ed.
18. 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. 5th ed.
19. 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. Proceedings of the National Academy of Sciences of the United States of America 1962, 48:1086-1092.
20. Creighton T.E. Proteins structures and molecular properties 1993, W.H. Freeman and Co, New York, 507. 2nd ed.
21. Eisenberg D. The discovery of the α-helix and the β-sheet, the principal structural features of proteins. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:11207-11210.
22. 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.
23. Judson H.F. The eighth day of creation 1979, Simon and Shuster, New York.
24. Moore P.B., Steitz T.A. The ribosome revealed. TIBS 2005, 30:281-283.
25. Perutz M.F. I wish I'd made you angry earlier. Essays on science, scientists and humanity 2002, Oxford University Press, 354.
26. Rodnina M.V., Beringer M., Wintermeyer W. How ribosomes make peptide bonds. TIBS 2007, 32:20-26.
27. Selmer M., Dunham C.M., Murphy F.V., Weixlbaumer A., Petry S., Kelley A.C., et al. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 2006, 313:1935-1943.
28. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken, 1591. 3rd ed.
29. Watson J.D., Crick F.H.C. Genetical implications of the structure of deoxyribonucleic acid. Nature 1953, 171:964-967.
30. Yonath A. Ribosomal crystallography: Peptide bond formation, chaperone assistance and antibiotics activity 2005.
31. 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.
32. Al-Karadaghi S., Franco R., Hansson M., Shelnutt J.A., Isaya G., Ferreira G.C. Chelatases: distort to select?. Trends in Biochemical Sciences 2006, 31:135-142.
33. Chu B.C., Garcia-Herrero A., Johanson T.H., Krewulak K.D., Lau C.K., Peacock R.S., et al. Siderophore uptake in bacteria and the battle for iron with the & host; a bird's eye view. Biometals 2010, 23:601-611.
34. Culotta V.C., Yang M., O'Halloran T.V.O. Activation of superoxide dismutases: putting the metal to the pedal. Biochimica et Biophysica Acta 2006, 1763:747-758.
35. Krewulak K.D., Vogel H.J. Structural biology of bacterial iron uptake. Biochim. Biophys Acta 2008, 1778:1781-1804.
36. Lee C.C., Blank M.A., Fay A.W., Yoshizawa J.M., Hu Y., Hodgson K.O., et al. Stepwise formation of P-cluster in nitrogenase MoFe protein. Proceedings of the National Academy of Sciences of the United States of America 2009, 106:18474-18478.
37. Mendel R.R., Smith A.G., Marquet A., Warren M.J. Metal and cofactor insertion. Natural Product Reports 2007, 24:963-971.
38. Miller M.C., Parkin S., Fetherson J.D., Perry R.D., Demoll E. Crystal structure of ferric-yersiniabactin, a virulence factor of, Yersinia pestis. Journal of Inorganic Biochemistry 2006, 100:1495-1500.
39. Nicolet Y., Cavazza C., Fontecilla-Camps J.-C. Fe-only hydrogenases: structure, function and evolution. Journal of Inorganic Biochemistry 2002, 91:1-8.
40. Rao P.V., Holm R.H. Synthetic analogues of the active sites of iron-sulfur proteins. Chemical Reviews 2004, 104:527-559.
41. Raymond K.N., Dertz E.A., Kim S.S. Enterobactin: an archetype for microbial iron transport. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:3584-3588.
42. Rees D.C. Great metalloclusters in enzymology. Annual Review of Biochemistry 2002, 71:221-246.
43. Roach P.L. Radicals from S-adenosylmethionine and their application to biosynthesis. Current Opinion in Chemical Biology 2010, 2010 Dec 13. (Epub ahead of print).
44. Rubio L.M., Ludden P.W. Biosynthesis of the iron-molybdenum cofactor of nitrogenase. Annual Review of Microbiology 2008, 62:93-111.
45. Schwarz G., Mendel R.R., Ribbe M.W. Molybdenum cofactors, enzymes and pathways. Nature 2009, 460:839-847.
46. Sheftel A., Stehling O., Lill R. Iron-sulfur proteins in health and disease. Trends in Endocrinology and Metabolism 2010, 21:302-314.
47. Zhou Z., Lai J.R., Walsh C.T. Directed evolution of aryl carrier proteins in the enterobactin synthetase. Proceedings of the National Academy of Sciences of the United States of America 2007, 104:11621-11626.
48. Abrahams K.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F, -ATPase from bovine heart mitochondria. Nature 1994, 370:621-628.
49. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2002, W.H. Freeman and Co., New York. 5th ed.
50. Campbell P.N., Smith A.D., Peters T.J. Biochemistry illustrated niochemistry and molecular biology in the post-genomic era 2005, Elsevier, London and Oxford, pp. 242. 5th ed.
51. 0-type ATP synthase, a biological rotary motor. TIBS 2002, 27:154-160.
52. Devlin T.M. Textbook of Biochemistry with clinical correlations 2005, John Wiley and Sons, Hoboken, pp. 1208. 6th ed.
53. Knowles J.R. Enzyme catalysis: not different, just better. Nature 1991, 350:121-124.
54. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken. 3rd ed.
55. Arnesano F., Banci L., Piccioli M. NMR structures of paramagnetic proteins. Quarterly Reviews of Biophysics 2005, 38:167-219.
56. Banci L., Bertini I., Cantini F., Felli I.C., Gonnelli L., Hadjiliadis N., et al. The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Nature Chemical Biology 2006, 2:367-368.
57. Bertini I., Luchinat C., Parigi G., Pierattelli R. NMR spectroscopy of paramagnetic metalloproteins. Chembiochem 2005, 6:1536-1549.
58. Campbell I.D., Dwek R.A. Biological spectroscopy 1984, Benjamin/Cummings Publishing Co., Inc, Menlo Park, Calif., pp. 404.
59. Carette N., Hagen W., Bertrand L., de Val N., Vertommen D., Roland F., et al. Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins. Journal of Inorganic Biochemistry 2006, 100:1426-1435.
60. Practical approaches to biological inorganic chemistry 2012, Elsevier. R.R. Crichton, R.O. Louro (Eds.).
61. Ealick S.E. Advances in multiple wavelength anomalous diffraction crystallography. Current Opinion in Chemical Biology 2000, 4:495-499.
62. Fragai M., Luchinat C., Parigi G. "Four-dimensional" protein structures: examples from metalloproteins. Accounts of Chemical Research 2006, 39:909-917.
63. Hagen W.R. EPR spectroscopy as a probe of metal centres in biological systems. Dalton Transactions 2006, 37:4415-4434.
64. Neese F. Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mössbauer properties. Current Opinion in Chemical Biology 2003, 7:125-135.
65. Que L. Physical methods in bioinorganic chemistry: Spectroscopy and magnetism 2000, University Science Books, Sausalito, Ca, pp. 59-120.
66. Ren B., Tibbelin G., Kajino T., Asami O., Ladenstein R. The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. Journal of Molecular Biology 2003, 329:467-477.
67. Strange R.W., Feiters M.C. Biological X-ray absorption spectroscopy (BioXAS): a valuable tool for the study of trace elements in the life sciences. Current Opinion in Structural Biology 2008, 18:609-616.
68. Toussaint L., Cuypers M.G., Bertrand L., Hue L., Romão C.V., Saraiva L.M., et al. Comparative Fe and Zn K-edge X-ray absorption spectroscopic study of the ferroxidase centres of human H-chain ferritin and bacterioferritin from desulfovibrio desulfuricans. Journal of Biological Inorganic Chemistry 2009, 14:35-49.
69. Ubbink M., Worrall J.A.R., Canters G.W., Groenen E.J.J., Huber R. Paramagnetic resonance of biological metal centers. Annual Review of Biophysics and Biomolecular Structure 2002, 31393-31422.
70. Ward R.J., Ramsey M., Dickson D.P., Hunt C., Douglas T., Mann S., et al. Further characterisation of forms of haemosiderin in iron-overloaded tissues. European Journal of Biochemistry 1994, 225:187-194.
71. Balasubramanian R., Rosenzweig A.C. Copper methanobactin: a molecule whose time has come. Current Opinion in Chemical Biology 2008, 12:245-249.
72. Chu B.C., Garcia-Herrero A., Johanson T.H., Krewulak K.D., Lau C.K., Peacock R.S., et al. Siderophore uptake in bacteria and the battle for iron with the & host; a bird's eye view. Biometals 2010, 23:601-611.
73. Cobine P.A., Pierrel F., Winge D.R. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochimica et Biophysica Acta 2006, 1763:759-772.
74. Crichton R.R. Inorganic biochemistry of iron metabolism: from molecular mechanisms to clinical consequences 2009, John Wiley and Sons, Chichester, pp 461. 3rd ed.
75. Eide D.J. The SLC39 family of metal ion transporters. Pflügers Archiv - European Journal of Physiology 2004, 447:796-800.
76. Eide D.J. Zinc transporters and the cellular trafficking of zinc. Biochimica et Biophysica Acta 2006, 1763:711-722.
77. 3+ reduction improves rice yields. Proceedings of the National Academy of Sciences USA 2007, 104:7311-7312.
78. Hantke K. Bacterial zinc transporters and regulators. Biometals 2001, 14:139-249.
79. Kosman D.J. Molecular mechanisms of iron uptake in fungi. Molecular Microbiology 2003, 47:1185-1197.
80. Krewulak K.D., Vogel H.J. Structural biology of bacterial iron uptake. Biochimica et Biophysica Acta 2008, 1778:1781-1804.
81. Kwok E.Y., Severance S., Kosman D.J. Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane. Biochemistry 2006, 45:6317-6327.
82. Martin J.H., Fitzwater S.E. Iron deficiency limits phytoplankton growth in the north-east Pacific subartic. Nature 1988, 331:341-343.
83. Palmer C.M., Guerinot M. Facing the challenges of Cu, Fe and Zn homeostasis in plants. Nature Chemical Biology 2009, 5:333-340.
84. Palmiter R.D., Huang L. Efflux and compartmentalisation of zinc by members of the SLC30 family of solute carriers. Pfluger's Arch. 2004, 447:744-751.
85. Petris M.J. The SLC31 (Ctr) copper transporter family. Pflügers Archiv - European Journal of Physiology 2004, 447:796-800.
86. Philpott C.C. Iron uptake in fungi: a system for every source. Biochimica et Biophysica Acta 2006, 1763:636-645.
87. Schmidt W. Iron solutions: acquisition strategies and signalling pathways in plants. Trends in Plant Science 2003, 8:188-193.
88. Shi D., Xu Y., Hopkinson B.M., Morel F.M.M. Effect of ocean acidification on iron availability to marine phytoplankton. Science 2010, 327:676-679.
89. Shi L., Squier T.C., Zachara J.M., Fredrickson J.K. Respiration of metal (hydr)oxides by, Shewanella and, Geobacter: a key role for multihaem c-type cytochromes. Molecular Microbiology 2007, 65:12-20.
90. Solioz M., Stoyanov J.V. Copper homeostasis in, Enterococcus hirae. FEMS Microbiology Reviews 2003, 27:183-195.
91. Vraspir J.M., Butler A. Chemistry of marine ligands and siderophores. Annual Review of Marine Science 2009, 1:43-63.
92. Andrews S.C., Robinson A.K., Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol. Rev 2003, 27:215-237.
93. Blindauer C.A. Zinc-handling in cyanobacteria: an update. Chemistry & Biodiversity 2008, 5:1990-2013.
94. Boal A.K., Rosenzweig A.C. Structural biology of copper trafficking. Chemical Reviews 2009, 109:4760-4779.
95. Chiancone E., Ceci P. The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding. Biochimica et Biophysica Acta 2010, 1800:798-805.
96. Cobine P.A., Pierrel F., Winge D.R. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochimica et Biophysica Acta 2006, 1763:759-772.
97. Crichton R.R. Inorganic biochemistry of iron metabolism: From molecular mechanisms to clinical consequences 2009, John Wiley and Sons, Chichester. 3rd ed.
98. Eide D.J. Zinc transporters and the cellular trafficking of zinc. Biochimica et Biophysica Acta 2006, 1763:711-722.
99. Grotz N., Guerinot M.L. Molecular aspects of Cu, Fe and Zn homeostasis in plants. Biochimica et Biophysica Acta 2006, 1763:595-608.
100. Lee J.W., Helmann J.D. Functional specialization within the Fur family of metalloregulators. Biometals 2007, 20:485-499.
101. Lill R., Dutkiewicz R., Elsässer H.P., Hausmann A., Netz D.J., Pierik A.J., et al. Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes. Biochimica et Biophysica Acta 2006, 1763:652-667.
102. Massé E., Salvail H., Desnoyers G., Arguin M. Small RNAs controlling iron metabolism. Current Opinion in Microbiology 2007, 10:140-145.
103. Palmer C.M., Guerinot M.L. Facing the challenges of Cu, Fe and Zn homeostasis in plants. Nature Chemical Biology 2009, 5:333-340.
104. Pilon M., Cohu C.M., Ravet K., Abdel-Ghany S.E., Gaymard F. Essential transition metal homeostasis in plants. Current Opinion in Plant Biology 2009, 12:347-357.
105. Richardson D.R., Lane D.J., Becker E.M., Huang M.L., Whitnall M., Rahmanto Y.S., Sheftel A.D., Ponka P. Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol. Proc Natl Acad Sci U S A 2010, 107:10775-10782.
106. Rouault T.A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nature Chemical Biology 2006, 2:406-414.
107. Schmidt W. Iron solutions: acquisition strategies and signaling pathways in plants. Trends in Plant Science 2003, 8:188-193.
108. Solioz M., Abicht H.K., Mermod M., Mancini S. Response of gram-positive bacteria to copper stress. The Journal of Biological Inorganic Chemistry 2010, 15:3-14.
109. Sutak R., Lesuisse E., Tachezy J., Richardson D.R. Crusade for iron: iron uptake in unicellular eukaryotes and its significance for virulence. Trends in Microbiology 2008, 16:261-268.
110. van den Berghe P.V., Klomp L.W. Posttranslational regulation of copper transporters. Journal of Biological Inorganic Chemistry 2010, 15:37-46.
111. Vaulont S., Lou D.-Q., Viatte L., Kahn A. Of mice and men: the iron age. The Journal of Clinical Investigation 2005, 115:2079-2082.
112. Walker E.L., Connolly E.L. Time to pump iron: iron-deficiency-signalling mechanisms of higher plants. Current Opinion in Plant Biology 2008, 11:530-535.
113. Wallander M.L., Leibold E.A., Eisenstein R.S. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochimica et Biophysica Acta 2006, 1763:668-689.
114. Watt R.K., Hilton R.J., Graff D.M. Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell. Biochimica et Biophysica Acta 2010, 1800:745-759.
115. 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 Research 2006, 34:2723-2735.
116. Bublitz M., Poulsen H., Morth J.P., Nissen P. In and out of the cation pumps: P-type ATPase structure revisited. Current Opinion in Structural Biology 2010, 20:431-439.
117. Catterall W.A. From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels. Neuron 2000, 26:13-25.
118. Dietrich B. Coordination chemistry of alkali and alkaline-earth cations with macrocyclic ligands, cations with macrocyclic ligands. The Journal of Chemical Education 1985, 62:954-964.
119. +conduction and selectivity. Science 1998, 280:69-77.
120. Gouaux E., MacKinnon Principles of selective ion transport in channels and pumps. Science 2005, 310:1461-1465.
121. Hodgkin A.L., Huxley A.F. A quantitative description of membrane current and its application to conduction and excitation in nerve. The Journal of Physiology 1952, 117:500-544.
122. Jiang J., Amara S.G. New views of glutamate transporter structure and function: advances and challenges. Neuropharmacol 2011, 60:172-181.
123. + exchanger 1 (NHE1): functional and clinical implications. J Biol Chem 2007, 282:37854-37863. "http://www.ncbi.nlm.nih.gov/pubmed/17981808".
124. MacKinnon R. Potassium channels and the atomic basis of selective ion conduction (Nobel Lecture). Angewandte Chemie International Edition 2004, 43:4265-4277.
125. Schushan M., Xiang M., Bogomiakov P., Padan E., Rao R., Ben-Tal N. Model-guided mutagenesis drives functional studies of human NHA2, implicated in hypertension. J Mol Biol 2010, 396:1181-1196.
126. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken. 3rd ed.
127. Yu F.H., Yarov-Yarovoy V., Gutman G.A., Catterall W.A. Overview of molecular relationships in the voltage-gated ion channel superfamily. Pharmacological Reviews 2005, 57:387-395.
128. Wozki S.A., Schmidt F.J. DNA and RNA: composition and structure. Textbook of biochemistry with clinical correlations 2002, 45-92. 5th ed. T.M. Devlin (Ed.).
129. Allen K.N., Dunaway-Mariano D. Phosphoryl group transfer: evolution of a catalytic scaffold. TIBS 2004, 29:495-503.
130. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2001, Freeman, New York. 5th ed.
131. Cowan J.A. Structural and catalytic chemistry of magnesium-dependent enzymes. BioMetals 2002, 15:225-235.
132. Frausto da Silva J.J.R., Williams R.J.P. The biological chemistry of the elements 2001, Oxford University Press, p. 270. 2nd ed.
133. Gerlt J.A., Babbitt P.C., Rayment I. Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Archives of Biochemistry and Biophysics 2005, 433:59-70.
134. Grueninger D., Schultz G.E. Structure and Reaction Mechanism of L-Rhamnulose Kinase from, Eschericia coli. Journal of Molecular Biology 2006, 359:787-797.
135. Knowles J.R. Enzyme-catalysed phosphoryl transfer reactions. The Annual Review of Biochemistry 1980, 49:877-919.
136. 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.
137. Maguire M.E., Cowan J.A. Magnesium chemistry and biochemistry. BioMetals 2002, 15:203-210.
138. Nowotny M., Yang W. Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release. EMBO Journal 2006, 25:1924-1933.
139. Peeraer Y., Rabijns A., Collet J.-F., Van Scaftingen E., De Ranter C. How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. European Journal of Biochemistry 2004, 271:3421-3427.
140. Schmidt B.H., Burgin A.B., Deweese J.E., Osheroff N., Berger J.M. A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases. Nature 2010, 465:641-644.
141. Steitz T.A., Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proceedings of the National Academy of Sciences of the United States of America 1993, 90:698-6502.
142. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, New York, Chichester. 3rd ed.
143. 2+-ion catalysis and substrate specificity. Molecular Cell 2006, 22:5-13.
144. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2001, Freeman, New York, 974. 5th ed.
145. Cahalan M.D. STIMulating store-operated Ca(2+) entry. Nature Cell Biology 2009, 11:669-677.
146. Carafoli E. The calcium cycle of mitochondria. FEBS Letters 1979, 104:1-5.
147. Carafoli E. Calcium signalling: a tale for all seasons. Proceedings of the National Academy of Sciences of the United States of America 2002, 99:1115-1122.
148. Carafoli E. Historical review: mitochondria and calcium: ups and downsof an unusual relationship. Trends in Biochemical Sciences 2003, 28:175-181.
149. Carafoli E. Calcium-mediated cellular signals: a story of failures. Trends in Biochemical Sciences 2004, 29:371-379.
150. Carafoli E. Calcium - a universal carrier of biological signals. FEBS Journal 2005, 272:1073-1089.
151. Clapham D.E. Calcium signaling. Cell 2007, 131:1047-1058.
152. Di Leva F., Domi T., Fedrizzi L., Lim D., Carafoli E. The plasma membrane Ca2+ ATPase of animal cells: structure, function and regulation. Archives of Biochemistry and Biophysics 2008, 476:65-74.
153. Guerini D., Coletto L., Carafoli E. Exporting calcium from cells. Cell Calcium 2005, 38:281-289.
154. Kurosaki T., Baba Y. Ca2+ signaling and STIM1. Progress in Biophysics and Molecular Biology 2010, 103:51-58.
155. Rizzuto R., Brini M., Murgia M., Pozzan T. Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 1993, 262:744-747.
156. Toyoshima C. Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum. Archives of Biochemistry and Biophysics 2008, 476:3-11.
157. Toyoshima C. How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane. Biochimica et Biophysica Acta 2009, 1793:941-946.
158. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, New York, Chichester. 3rd ed.
159. Williams R.J.P. The evolution of calcium biochemistry. Biochimica et Biophysica Acta 2006, 1763:1139-1146.
160. Auld D.S. Zinc coordination sphere in biochemical zinc sites. BioMetals 2001, 14:271-313.
161. Bebrone C. Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochemical Pharmacology 2007, 74:1686-1701.
162. Brown R.S. Zinc finger proteins: getting a grip on RNA. Current Opinion in Chemical Biology 2005, 15:94-98.
163. Gross J. How tadpoles lose their tails: path to discovery of the first matrix metalloproteinase. Matrix Biol 2004, 23:3-13.
164. Hall T.M. Multiple modes of RNA recognition by zinc finger proteins. Current Opinion in Chemical Biology 2005, 15:367-373.
165. Holz R.C., Bzymek K.P., Swierczek S.I. Co-catalytic metallopeptidases as pharmaceutical targets. Current Opinion in Chemical Biology 2003, 7:197-206.
166. Kavanagh K.L., Jörnvall H., Persson B., Oppermann U. Medium- and short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cellular and Molecular Life Sciences 2008, 65:3895-3906.
167. Klug A., Rhodes D. 'Zinc fingers': a novel protein motif for nucleic acid recignition. TIBS 1987, 12:464-469.
168. McCall K.A., Huang C.-C., Fierke C.A. Function and mechanism of zinc metalloenzymes. Journal of Nutrition 2000, 130:1437S-1446S.
169. Parkin G. Synthetic analogues relevant to the structure and function of zinc enzymes. Chemical Reviews 2004, 104:699-767.
170. Tallant C., Marrero A., Gomis-Rüth F.X. Matrix metalloproteinases: fold and function of their catalytic domains. Biochimica et Biophysica Acta 2010, 1803:20-28.
171. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, New York, Chichester, p. 1360. 3rd ed.
172. Wu S., Zhang C., Xu D., Guo H. Catalysis of carboxypeptidase A: promoted-water versus nucleophilic pathways. Journal of Physical Chemistry B 2010, 114:9259-9267.
173. Andreou A., Feussner I. Lipoxygenases - structure and reaction mechanism. Phytochemistry 2009, 70:644-649.
174. Atta M., Mulliez E., Arragain S., Forouhar F., Hunt J.F., Fontecave M. S-Adenosylmethionine-dependent radical-based modification of biological macromolecules. Current Opinion in Structural Biology 2010, 20:684-692.
175. Brzezinski P., Johansson A.L. Variable proton-pumping stoichiometry in structural variants of cytochrome c oxidase. Biochimica et Biophysica Acta 2010, 1797:710-713.
176. Collman J.P., Boulatov R., Sunderland C.J., Fu I. Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. Chemical Reviews 2004, 104:561-588.
177. Crichton R.R., Pierre J.-L. Old iron, young copper: from Mars to venus. Biometals 2001, 14:99-112.
178. Dempsey J.L., Esswein A.J., Manke D.R., Rosenthal J., Soper J.D., Nocera D.G. Molecular chemistry of consequence to renewable energy. Inorganic Chemistry 2005, 44:6879-6892.
179. Fenton H.J.H. Transactions of the Chemical Society 1894, 65:899-910.
180. Fontecave M., Atta M., Mulliez E. S-adenosylmethionine: nothing goes to waste. TIBS 2004, 29:243-249.
181. Gelin B.R., Karplus M. Mechanism of tertiary structural change in hemoglobin. Proceedings of the National Academy of Sciences of the United States of America 1977, 74:801-805.
182. Haber F., Weiss J. The catalytic decomposition of hydrogen peroxide by iron salts. Proceedings of the Royal Society of London - Series A 1934, 147:332-351.
183. Hosler J.P., Ferguson-Miller S., Mills D.A. Energy transduction: proton transfer through the respiratory complexes. Current Opinion in Structural Biology 2006, 17:444-450.
184. Huber C., Wächtershäuser G. α-Hydroxy and α-amino acids under possible Hadean, volcanic origin-of-life conditions. Science 2006, 314:630-632.
185. Hunte C., Koepke J., Lange C., Rossmanith T., Michel H. Structure at 2.3 Å resolution of the cytochrome bc1 complex from the yeast, Saccharomyces cerevisiae with an antibody FV fragment. Structure 2000, 8:669-684.
186. Hunte C. Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragments. FEBS Letters 2001, 504:126-132.
187. 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. Journal of Biological Chemistry 2002, 277:16124-16130.
188. Keilin D. On cytochrome, a respiratory pigment, common to animals, yeast, and higher plants. Proceedings of the Royal Society of London - Series B: Biological Sciences 1925, 98:312-339.
189. Koehntop K.D., Emerson J.P., Que L. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. Journal of Biological Inorganic Chemistry 2005, 10:87-93.
190. Krebs C., Fujimori D.G., Walsh C.T., Bollinger J.M. Non-heme Fe(IV)-oxo intermediates. Accounts of Chemical Research 2007, 40:484-492.
191. Kurz D.M. Structural similarity and functional diversity in diiron-oxo proteins. The Journal of Biological Inorganic Chemistry 1997, 2:159-167.
192. Johnston J.B., Ouellet H., Podust L.M., Ortiz de Montellano P.R. Structural control of cytochrome P450-catalyzed ω-hydroxylation. Archives of Biochemistry and Biophysics 2011, 507:86-94.
193. Lange S.J., Que L. Oxygen activating nonheme iron enzymes. Current Opinion in Chemical Biology 1998, 2:159-172.
194. Lim J.H., Yu Y.G., Han Y.S., Cho S., Ahn B.Y., Kim S.H., et al. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability. Journal of Molecular Biology 1997, 270:259-274.
195. Lipscomb J.D. Mechanism of extradiol aromatic ring-cleaving dioxygenases. Current Opinion in Structural Biology 2008, 18:644-649.
196. McMunn C.A. On myohaematin, an intrinsic muscle-pigment of vertebrates and invertebrates, on histohaematin, and on the spectrum of the suprarenal bodies. The Journal of Physiology 1884, 5:XXIV.
197. Nordlund P., Eklund H. Di-iron-carboxylate proteins. Current Opinion in Structural Biology 1995, 5:758-766.
198. Nordlund P., Reichard P. Ribonucleotide reductases. The Annual Review of Biochemistry 2006, 75:681-706.
199. Poulos T.L., Finzel B.C., Howard A.J. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 1986, 25:5314-5322.
200. Qin L., Hiser C., Mulichak A., Garavito R.M., Ferguson-Miller S. Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome, c oxidase. Proceedings of the National Academy of Sciences of the United States of America 2006, 103:16117-16122.
201. Rao P.V., Holm R.H. Synthetic analogues of the active sites of iron-sulfur proteins. Chemical Reviews 2004, 104:527-559.
202. Reece S.Y., Hodgkiss J.M., Stubbe J., Nocera S.G. Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology. Philosophical Transactions of the Royal Society B: Biological Sciences 2006, 361:1351-1364.
203. Rees D.C. Great metalloclusters in enzymology. Annual Review of Biochemistry 2002, 71:221-246.
204. Stubbe J., Ge J., Yee C.S. The evolution of ribonucleotide reduction revisited. TIBS 2001, 26:93-99.
205. Sazinsky M.H., Lippard S.J. Correlating structure with function in bacterial multicomponent monooxygenases and related diiron proteins. Accounts of Chemical Research 2006, 39:558-566.
206. nY356-R2s (n = 2, 3, 4) in E. coli ribonucleotide reductase: evidence that Y356 is a redox active amino acid along the radical propagation pathway. Journal of the American Chemical Society 2006, 128:1562-1568.
207. Stubbe J., Nocera D.G., Yee C.S., Chang M.Y.C. Radical initiation in the class I ribonucleotide reductase: longrange proton-coupled electron transfer?. Chemical Reviews 2003, 103:2167-2202.
208. Stubbe J., Riggs-Gelasco P. Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase. TIBS 1998, 23:438-443.
209. Uhlin U., Eklund H. Structure of ribonucleotide reductase protein R1. Nature 1994, 370:533-539.
210. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken, N.J. 3rd ed.
211. Balasubramanian R., Smith S.M., Rawat S., Yatsunyk L.A., Stemmler T.L., Rosenzweig A.C. Oxidation of methane by a biological dicopper centre. Nature 2010, 465:115-119.
212. Brunori M., Giuffrè A., Sarti P. Cytochrome, c oxidase, ligands and electrons. Journal of Inorganic Biochemistry 2005, 99:324-336.
213. Z cluster active site. Angewandte Chemie International Edition 2004, 43:4132-4140.
214. Crichton R.R. Inorganic biochemistry of iron metabolism: From molecular mechanisms to clinical consequences 2001, John Wiley and Sons, Chichester, pp. 326.
215. Crichton R.R., Pierre J.-L. Old iron, young copper: from Mars to Venus. BioMetals 2001, 14:99-112.
216. Crichton R.R., Ward R.J. Metal-based neurodegeneration from molecular mechanisms to therapeutic strategies 2006, John Wiley and Sons, Chichester, p. 227.
217. Decker H. A first crystal structure of tyrosinase: all questions answered?. Angewandte Chemie International Edition 2006, 45:4546-4550.
218. Decker H., Schweikardt T., Nillius D., Salzbrunn U., Jaenicke E., Tuczek F. Gene 2007, 398:183-191.
219. Granata A., Monzani E., Casella L. Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complex. Journal of Biological Inorganic Chemistry 2004, 9:189-196.
220. Hart P.J. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Current Opinion in Chemical Biology 2006, 10:131-138.
221. 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.
222. 2 structure and subsequent reactivity. Journal of Biological Inorganic Chemistry 2004, 9:669-683.
223. Hellman N.E., Gitlin J.D. Ceruloplasmin metabolism and function. Annual Review of Nutrition 2002, 22:439-458.
224. Himes R.A., Karlin K.D. Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO). Current Opinion in Chemical Biology 2009, 13:119-131.
225. Klinman J.P. The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation. Journal of Biological Chemistry 2006, 281:3013-3016.
226. Malkin R., Malmström B.G. The state and function of copper in biological systems. Advances in Enzymology and Related Areas of Molecular Biology 1970, 33:177-244.
227. Handbook of metalloproteins 2001, 227. John Wiley and Sons, Chichester. A. Messerschmidt, R. Huber, T. Poulos, K. Weighardt (Eds.).
228. Potter S.Z., Valentine J.S. The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). Journal of Biological Inorganic Chemistry 2003, 8:373-380.
229. Riva S. Laccases: blue enzymes for green chemistry. TIBS 2006, 24:219-226.
230. Rodgers C.J., Blanford C.F., Giddens S.R., Skamnioto P., Armstrong F.A., Gurr S.J. Designer laccases: a vogue for higpotential fungal enzymes?. Trends in Biotechnology 2009, 28:63-72.
231. Rogers M.S., Dooley D.M. Copper-tyrosyl enzymes. Current Opinion in Structural Biology 2003, 7:131-138.
232. Rosenzweig A.C., Sazinsky M.H. Structural insights into dioxygen-activating copper enzymes. Current Opinion in Structural Biology 2006, 16:729-735.
233. Solomon E.I. Spectroscopic methods in bioinorganic chemistry: blue to red to green copper sites. Inorganic Chemistry 2006, 45:8012-8025.
234. Vallee B.L., Williams R.J. Metalloenzymes: the entatic nature of their active sites. Proceedings of the National Academy of Sciences of the United States of America 1968, 59:498-505.
235. 12: catalysis by cobalamin-dependent enzymes. The Annual Review of Biochemistry 2003, 72:209-247.
236. 12 trafficking. Current Opinion in Chemical Biology 2009, 13:484-491.
237. 12. Chemical Reviews 2005, 105:2075-2149.
238. Drennan C.L., Doukov T.I., Ragsdale S.W. The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures. The Journal of Biological Inorganic Chemistry 2004, 9:511-515.
239. El Fantroussi S., Naveau H., Agathos S.N. Anaerobic dechlorinating bacteria. Biotechnol Progress 1998, 14:167-188.
240. Hegg E.L. Unravelling the structure and mechanism of acetyl-coenzyme A synthase. Accounts of Chemical Research 2004, 37:775-783.
241. Kobayashi M., Shimizu Cobalt proteins. European Journal of Biochemistry 1999, 261:1-9.
242. Lill S.O., Siegbahn P.E. An autocatalytic mechanism for NiFe-hydrogenase: reduction to Ni(I) followed by oxidative addition. Biochemistry 2009, 48:1056-1066.
243. Lowther W.T., Matthews B.W. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chemical Reviews 2002, 102:4581-4607.
244. Mulrooney S.B., Hausinger R.P. Nickel uptake and utilisation by microorganisms. FEMS Microbiology Reviews 2003, 27:239-269.
245. Ragsdale S.W. Nickel biochemistry. Current Opinion in Chemical Biology 1998, 2208-2215.
246. Ragsdale S.W. Life with carbon monoxide. Critical Reviews in Biochemistry and Molecular Biology 2004, 39:165-195.
247. Ragsdale S.W. Metals and their scaffolds to promote difficult enzymatic reactions. Chemical Reviews 2006, 106:3317-3337.
248. Ragsdale S.W. Nickel and the carbon cycle. Journal of Inorganic Biochemistry 2007, 101:1657-1666.
249. Ragsdale S.W. Nickel-based enzyme systems. Journal of Biological Chemistry 2009, 284:18571-18575.
250. Ragsdale S.W., Pierce E. Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation. Biochimica et Biophysica Acta 2008, 1784:1873-1898.
251. Reed G.H. Radical mechanisms in adenosylcobalamin-dependent enzymes. Current Opinion in Chemical Biology 2004, 8:477-483.
252. 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. Journal of Bioscience and Bioengineering 2002, 93:519-530.
253. Svetlitchnyi V., Dobbek H., Meyer-Klauke W., Meins T., Thiele B., Römer P., et al. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proceedings of the National Academy of Sciences of the United States of America 2004, 101:446-451.
254. Thauer R.K., Kaster A.K., Seedorf H., Buckel W., Hedderich R. Methanogenic archaea: ecologically relevant differences in energy conservation. Nature Reviews Microbiology 2008, 6:579-591.
255. 2 storage. The Annual Review of Biochemistry 2010, 79:507-536.
256. Ash D.E. Arginine metabolism: enzymology, nutrition and clinical significance. Journal of Nutrition 2004, 134:2760S-2764S.
257. Barber J. Photosynthetic generation of oxygen. Philosophical Transactions of the Royal Society B: Biological Sciences 2008, 363:2665-2674.
258. 2+ cluster of photosystem II and its protein environment as revealed by X-ray crystallography. Philosophical Transactions of the Royal Society B: Biological Sciences 2008, 363:1129-1138.
259. Barynin V.V., Whittaker M.M., Antonyuk S.V., Lamzin V.S., Harrison P.M., Artymiuk P.J., et al. Crystal Structure of Manganese Catalase from Lactobacillus plantarum. Structure 2001, 9:725-738.
260. Christianson D.W. Arginase: structure, mechanism, and physiological role in male and female sexual arousal. Accounts of Chemical Research 2005, 38:191-201.
261. Cox J.D., Cama E., Colleluori D.M., Pethe S., Boucher J.-L., Mansuy D., et al. Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase. Biochemistry 2001, 40:2689-2701.
262. Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S. Architecture of the photosynthetic oxygen-evolving center. Science 2004, 303:1831-1838.
263. Goussias C., Boussac A., Rutherford A.W. Photosystem II and photosynthetic oxidation of water: an overview. Philosophical Transactions of the Royal Society B: Biological Sciences 2002, 357:1369-1381.
264. Iverson T.M. Evolution and unique bioenergetic mechanisms in oxygenic photosynthesis. Current Opinion in Chemical Biology 2006, 10:91-100.
265. Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W. Structure of a unique binuclear manganese cluster in arginase. Nature 1996, 383:554-557.
266. Loll B., Kern J., Saenger W., Zouni A., Biesiadka J. Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosytstem II. Nature 2005, 438:1040-1044.
267. Miller A.-F. Superoxide dismutases: active sites that save, but a protein that kills. Current Opinion in Chemical Biology 2004, 8:162-168.
268. Murray J.W., Barber J. Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel. Journal of Structural Biology 2007, 159:228-237.
269. Rutherford A.W., Boussac A. Water photolysis in biology. Science 2004, 303:1782-1784.
270. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken. 3rd ed.
271. Whittaker M.M., Barynin V.V., Igarashi T., Whittaker J.W. Outer sphere mutagenesis of, Lactobacillus plantarum manganese catalase disrupts the cluster core. Mechanistic implications. European Journal of Biochemistry 2003, 270:1102-1116.
272. Wu A.J., Penner-Hahn J.E., Pecoraro V.L. Structural, spectroscopic, and reactivity models for the manganese catalases. Chemical Reviews 2004, 104:903-938.
273. Brondino C.D., Romao M.J., Moura I., Moura J.J.G. Molybdenum and tungsten enzymes: the xanthine oxidase family. Current Opinion in Chemical Biology 2006, 10:109-114.
274. Butler A., Carter-Franklin J.N. The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products. Natural Product Reports 2004, 21:180-188.
275. Chatt J., Dilworth J.R., Richards R.L. Recent advances in the chemistry of nitrogen fixation. Chemical Reviews 1978, 78:589-625.
276. Chen Y., Watson H.M., Gao J., Sinha S.H., Cassady C.J., Vincent J.B. Characterization of the organic component of low-molecular-weight chromium-binding substance and its binding of chromium. Journal of Nutrition 2011, 141:1225-1232.
277. Crans D.C., Smee J.J., Gaidamauskas E., Yang L. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chemical Reviews 2004, 104:849-902.
278. Di Bona K.R., Love S., Rhodes N.R., McAdory D., Sinha S.H., Kern N., et al. Chromium is not an essential trace element for mammals: effects of a "low-chromium" diet. The Journal of Biological Inorganic Chemistry 2011, 16(3):381-390.
279. Downie J.A. Legume haemoglobins: symbiotic nitrogen fixation needs bloody nodules. Current Biology 2005, 15:R196-198.
280. 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. Chemical Reviews 2004, 104:1175-1200.
281. Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proceedings of the National Academy of Sciences of the United States of America 2000, 97:10723-10728.
282. Hidai M. Chemical nitrogen fixation by molybdenum and tungsten complexes. Coordination Chemistry Reviews 1999, 185-186:99-108.
283. Hille R. Molybdenum and tungsten in biology. TIBS 2002, 27:360-367.
284. Hille R. Molybdenum-containing hydroxylases. Archives of Biochemistry and Biophysics 2005, 433:107-116.
285. 2? A mechanistic overview of biological nitrogen fixation. Proceedings of the National Academy of Sciences of the United States of America 2006, 103:17088-17093.
286. Johnson-Winters K., Tollin G., Enemark J.H. Elucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses. Biochemistry 2010, 49:7242-7254.
287. Lau F.C., Bagchi M., Sen C.K., Bagchi D. Nutrigenomic basis of beneficial effects of chromium(III) on obesity and diabetes. Mol Cell Biochem 2008, 317:1-10.
288. Ligtenbarg A.G.J., Hage R., Feringa B.L. Catalytic oxidations by vanadium complexes. Coordination Chemistry Reviews 2003, 237:87-101.
289. Mendel R.R., Bittner F. Cell biology of molybdenum. Biochimica et Biophysica Acta 2006, 1763:621-635.
290. Michibata H., Yamaguchi N., Uyama T., Ueki T. Molecular biological approaches to the accumulation and reduction of vanadium by ascidians. Coordination Chemistry Reviews 2003, 237:41-51.
291. Nielsen F. Contreversial chromium: does the superstar mineral of the mountebanks receive appropriate attention from clinicians and nutritionists?. Nutrition Today 1996, 31:226-233.
292. Ohshiro T., Littlechild J., Garcia-Rodriguez E., Isupov M.N., Iida Y., Kobayashi T., et al. Modification of halogen specificity of a vanadium-dependent bromoperoxidase. Protein Science 2004, 13:1566-1571.
293. Peters J.W., Szilagyi R.K. Exploring new frontiers of nitrogenase structure and function. Current Opinion in Chemical Biology 2006, 10:101-108.
294. Rees D.C., Tezcan F.A., Haynes C.A., Walton M.Y., Andrade S., Einsle O., et al. Structural basis of biological nitrogen fixation. The Philosophical Transactions of the Royal Society 2005, 363:971-984.
295. Schrock R.R. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Accounts of Chemical Research 2005, 38:955-962.
296. Seefeldt L.C., Hoffman B.M., Dean D.R. Mechanism of Mo-dependent nitrogenase. The Annual Review of Biochemistry 2009, 78:701-722.
297. Ueki T., Furano N., Michibata H. A novel vanadium transporter of the Nramp family expressed at the vacuole of vanadium-accumulating cells of the ascidian Ascidia sydneiensis samea. Biochimica et Biophysica Acta 2011, 1810:457-464.
298. Vincent J.B. The biochemistry of chromium. The Journal of Nutrition 2000, 130:715-718.
299. Vincent J.B. Elucidating a biological role for chromium at a molecular level. Accounts of Chemical Research 2000, 33:503-510.
300. Vincent J.B. The potential value and potential toxicity of chromium picolinate as a nutritional supplement, weight-loss agent and muscle development agent. Sports Medicine 2003, 33:213-230.
301. Vincent J.B. Recent advances in the nutritional biochemistry of trivalent chromium. Proceedings of the Nutrition Society 2004, 63:41-47.
302. Voet D., Voet J.G. Biochemistry 2004, John Wiley and Sons, Hoboken, p. 1591. 3rd ed.
303. Yandulov D.V., Schrock R.R. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Science 2003, 301:76-78.
304. Allmang C., Wurth L., Krol A. The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated. Biochimica et Biophysica Acta 2009, 1790:1415-1423.
305. Arnér E.S.J. Selenoproteins - what unique properties can arise with selenocysteine in place of cysteine?. Experimental Cell Research 2010, 316:1296-1303.
306. Arrhenius S. On the influence of carbonic acid in the air on the temperature on the ground. Philosophical Magazine and Journal of Science 1896, 41:237.
307. Canfield D.C., Glazer A.N., Falkowski G.T. The evolution and future of Earth's nitrogen cycle. Science 2010, 330:192-196.
308. Dutzler R., Campbell E.B., MacKinnon R. Gating the selectivity filter in ClC chloride channels. Science 2003, 300:108-112.
309. Falkowski P.G., Fenchel T., Delong E.F. The microbial engines that drive earth's biogeochemical cycles. Science 2008, 320:1034-1039.
310. Flohé L. The labour pains of biochemical selenology: the history of selenoprotein biosynthesis. Biochimica et Biophysica Acta 2009, 1790:1389-1403.
311. Climate change 2007. Climate change impacts, adaptation and vulnerability 2007, Intergovermental Panel on Climate Change, Working Group II, IPCC, Geneva, Switzerland.
312. Lal R. Carbon sequestration. The Philosophical Transactions of the Royal SocietyB: Biological Sciences 2008, 303:815-820.
313. Lu J., Holmgren A. Selenoproteins. Journal of Biological Chemistry 2009, 284:723-727.
314. Muallem D., Vergani P. Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator. The Philosophical Transactions of the Royal SocietyB: Biological Sciences 2009, 364:247-255.
315. Rokita S.E., Adler J.M., McTamney P.M., Watson J.A. Efficient use and recycling of the micronutrient iodide in mammals. Biochimie 2010, 92:1227-1235.
316. Wessjohann L.A., Schneider A., Abbas M., Brandt W. Selenium in chemistry and biochemistry in comparison to sulfur. Biological Chemistry 2007, 388:997-1006.
317. Greenhouse gas bulletin: the state of greenhouse gases in the atmosphere using global observations up to December 2004 2006, WMO, World Meteorological Organization, Geneva, Switzerland.
318. Bou-Abdallah F. The iron redox and hydrolysis chemistry of the ferritins. Biochimica et Biophysica Acta 2010, 1800:719-731.
319. Crichton R.R., Declercq J.P. X-ray structures of ferritins and related proteins. Biochimica et Biophysica Acta 2010, 1800:706-718.
320. Crichton R.R., Roman F. A novel mechanism for ferritin iron oxidation and deposition. J. Mol. Catal. 1978, 4:75-82.
321. Gálvez N., Sánchez P., Domínguez-Vera J.M. Preparation of Cu and CuFe Prussian Blue derivative nanoparticles using the apoferritin cavity as nanoreactor. Dalton Trans. 2005, 7:2492-2494.
322. Jogler C., Schüler D. Genomics, genetics, and cell biology of magnetosome formation. The Annual Review of Microbiology 2009, 63:501-521.
323. Komeili A. Molecular mechanisms of magnetosome formation. The Annual Review of Biochemistry 2007, 76:351-366.
324. Kröger N., Poulsen N. Diatoms-from cell wall biogenesis to nanotechnology. Annual Review of Genetics 2008, 42:83-107.
325. LaMer V.K., Dinegar R.H.J. Theory, production and mechanism of formation of monodispersed hydrosols. Journal of the American Chemical Society 1950, 72:4847-4854.
326. Le Brun N.E., Crow A., Murphy M.E., Mauk A.G., Moore G.R. Iron core mineralisation in prokaryotic ferritins. Biochimica et Biophysica Acta 2010, 1800:732-744.
327. Lewin A., Moore G.R., Le Brun N.E. Formation of protein-coated iron minerals. Dalton Trans. 2005, 21:3597-3610.
328. Mann S., Webb J., Williams R.J.P. Biomineralization chemical and biochemical perspectives 1989, VCH, Wienheim.
329. Matsunaga T., Okamura Y. Genes and proteins involved in bacterial magnetic particle formation. Trends in Microbiology 2003, 11:536-541.
330. Meldrum F.C., Cölfen H. Controlling mineral morphologies and structures in biological and synthetic systems. Chemical Reviews 2008, 108:4332-4432.
331. Michel F.M., Ehm L., Antao S.M., Lee P.L., Chupas P.J., Liu G., et al. The structure of ferrihydrite, a nanocrystalline material. Science 2007, 316:1726-1729.
332. Müller W.E., Wang X., Cui F.Z., Jochum K.P., Tremel W., Bill J., et al. Sponge spicules as blueprints for the biofabrication of inorganic-organic composites and biomaterials. Applied Microbiology and Biotechnology 2009, 83:397-413.
333. Nyman J.S., Reyes M., Wang X. Effect of ultrastructural changes on the toughness of bone. Micron 2005, 36:566-582.
334. Thompson D.W. On growth and form 1942, Cambridge University Press Cambridge, pp. 1116.
335. 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. Journal of Molecular Biology 2007, 365:440-452.
336. Uchida M., Kang S., Reichhardt C., Harlen K., Douglas T. The ferritin superfamily: supramolecular templates for materials synthesis. Biochimica et Biophysica Acta 2010, 1800:834-845.
337. Wilt F.H. Developmental biology meets materials science: morphogenesis of biomineralized structures. Developmental Biology 2005, 280:15-25.
338. Abbott N.J., Patabendige A.A., Dolman D.E., Yusof S.R., Begley D.J. Structure and function of the blood-brain barrier. Neurobiology of Disease 2009, 37:13-25.
339. Bitanihirwe B.K.Y., Cunningham M.G. Zinc: the brain's dark horse. Synapse 2009, 63:1029-1049.
340. Cole T.B., Wenzel H.J., Kafer K.E., Schwartzkroin P.A., Palmiter R.D. Elimination of zinc from the synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene. Proceedings of the National Academy of Sciences of the United States of America 1999, 96:1716-1721.
341. Cousins R.J., Liuzzi J.P., Litchten L.A. Mammalian zinc transporters, trafficking and signals. Journal of Biological Chemistry 2006, 281:24085-24089.
342. Deisseroth K., Mermelstein P.G., Xia H., Tsien R.W. Signalling from synapse to nucleus: the logic behind the mechanisms. Current Opinion in Neurobiology 2003, 13:354-365.
343. Kuo Y.M., Zhou B., Cosco D., Gitschier J. The copper transporter Ctr1 provides an essential function in mammalian embryonic development. Proceedings of the National Academy of Sciences of the United States of America 2001, 98:220-225.
344. Lee J., Prohaska J.R., Thiele D.J. Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proceedings of the National Academy of Sciences of the United States of America 2001, 98:6842-6847.
345. Lodish D., Baltimore D., Berk A., Zipursky S.L., Matsudaira P., Darnell J. Molecular Cell Biology 1995, Scientific American Books, New York, p. 1344.
346. Paoletti P., Vergnano A.M., Barbour B., Casado M. Zinc at the glutamatergic synapses. Neuroscience 2009, 158:126-136.
347. 2+ sensitivity of high and low voltage activated calcium channels. Biophysical Journal 2007, 93:1175-1183.
348. Takeda A., Tamana H. Zinc signalling through glucocorticoid and glutamate signalling in stressful circumstances. Journal of Neuroscience Research 2010, 88:3002-3010.
349. Vacher H., Mohapatra D.P., Trimmer J.S. Localization and targeting of voltage-dependent ion channels in mammalian central neurons. Physiological Reviews 2008, 88:1407-1447.
350. Altamura S., Muckenthaler M.U. Iron toxicity in diseases of aging: Alzheimer's disease, Parkinson's disease and atherosclerosis. The Journal of Alzheimer's Disease 2009, 16:879-895.
351. Barzilai A., Melamed E. Molecular mechanisms of selective dopaminergic neuronal death in Parkinson's disease. Trends in Molecular Medicine 2003, 9:126-132.
352. Catala A. Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chemistry and Physics of Lipids 2009, 157:1-11.
353. Crichton R.R., Ward R.J. Metal based neurodegeneration: From molecular mechanisms to therapeutic strategies 2006, John Wiley & Sons, Chichester, pp. 227.
354. Dalle-Donne I., Giustarini D., Colombo R., Rossi R., Milzani A. Protein carbonylation in human diseases. Trends in Molecular Medicine 2003, 9:164-176.
355. Dürr A. Friedreich's ataxia: treatment within reach. The Lancet Neurology 2002, 1:370-374.
356. Duce J.A., Bush A.I. Biological metals and Alzheimer's disease: implications for therapeutics and diagnostics. Progress in Neurobiology 2010, 92:1-18.
357. Rogers J.T., Randall J.D., Cahill C.M., Eder P.S., Huang X., Gunshin H., et al. An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript. The Journal of Biological Chemistry 2002, 277:45518-45528.
358. Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nature Medicine 2004, 10:S10-17.
359. Schneider C., Porter N.A., Brash A.R. Routes to 4-hydroxynonenal: fundamental issues in the mechanisms of lipid peroxidation. J Biol Chem. 2008, 283:15539-15543.
360. Shaw B.F., Valentine J.S. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?. Trends in Biochemical Sciences 2007, 32:78-85.
361. Zecca L., Youdim M.B., Riederer P., Connor J.R., Crichton R.R. Iron, brain ageing and neurodegenerative disorders. Nat. Rev. Neurosci. 2004, 5:863-873.
362. Aime S., Frullano L., Geninatti Crich S. Compartmentalization of a gadolinium complex in the apoferritin cavity: a route to obtain high relaxivity contrast agents for magnetic resonance imaging. Angewandte Chemie International Edition 2002, 41:1017-1019.
363. Andrews N.C. Forging a field: the golden age of iron biology. Blood 2008, 112:219-230.
364. Brabec V., Kasparkova J. Platinum-based drugs. Metallo-therapeutic drugs and metal-based diagnostic agents. The use of metals in medicine 2005, 489-506. John Wiley and Sons, Chichester. M. Gielen, E.R. Tiekink (Eds.).
365. Crichton R.R., Ward R.J. Metal based neurodegeneration: From Molecular Mechanisms to Therapeutic Strategies 2006, John Wiley & Sons, Chichester, p. 227.
366. Dzik-Jurasz A.S.K. Molecular imaging, in vivo: an introduction. British Journal of Radiology 2003, 76:S98-S109.
367. Geninatti Crich S., Bussolati B., Tei L., Grange C., Esposito G., Lanzardo S., et al. Magnetic resonance visualization of tumor angiogenesis by targeting neural cell adhesion molecules with the highly sensitive gadolinium-loaded apoferritin probe. Cancer Research 2006, 66:9196-9201.
368. Gielen M., Tiekink E.R. Metallotherapeutic drugs and metal-based diagnostic agents. The use of metals in medicine 2005, John Wiley and Sons, Chichester, pp. 598.
369. Hartinger C.G., Zorbas-Seifried S., Jakupec M.A., Kynast B., Zorbas H., Keppler B.K. From bench to bedside-preclinical and early clinical development of the anticancer agent indazolium trans-[tetrachlorobis(1H-indazole)ruthenate(III)] (KP1019 or FFC14A). Journal of Inorganic Biochemistry 2006, 100:891-904.
370. Hershko C. Oral iron chelators: new opportunities and new dilemmas. Haematlogica 2006, 91:1307-1312.
371. Kálmán F.K., Geninatti-Crich S., Aime S. Reduction/dissolution of a beta-MnOOH nanophase in the ferritin cavity to yield a highly sensitive, biologically compatible magnetic resonance imaging agent. Angew Chem Int Ed Engl. 2010, 49:612-615.
372. Longueville A., Crichton R.R. An animal model of iron overload and its application to study hepatic ferritin iron mobilization by chelators. Biochemical Pharmacology 1986, 35:3669-3678.
373. McCance R.A., Widdowson E.M. Absorption and excretion of iron. Lancet 1937, II:680-684.
374. Meade T.J., Taylor A.K., Bull S.R. New magnetic resonance contrast agents as biochemical reporters. Current Opinion in Neurobiology 2003, 13:597-602.
375. Mota de Freitas D., Castro M.M., Geraldes C.F. Is competition between Li+ and Mg2+ the underlying theme in the proposed mechanisms for the pharmacological action of lithium salts in bipolar disorder?. Accounts of Chemical Research 2006, 39:283-291.
376. Nick H., Acklin P., Lattmann R., Buehlmayer P., Hauffe S., Schupp J., et al. Development of tridentate iron chelators: from desferrithiocin to ICL670. Current Medicinal Chemistry 2003, 10:1065-1076.
377. Pietrangelo A. Hemochromatosis: an endocrine liver disease. Hepatology 2007, 46:1291-1301.
378. Reedijk J. New clues for platinum antitumor chemistry: kinetically controlled meta binding to DNA. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:3611-3616.
379. Schmidt P.J., Toran P.T., Giannetti A.M., Bjorkman P.J., Andrews N.C. The transferrin receptor modulates Hfe-dependent regulation of hepcidin expression. Cell Metabolism 2008, 7:205-214.
380. Sigel A., Sigel H. Metal ions and their complexes in medication. Metal Ions in Biological Systems 2004, 41:519.
381. Terreno E., Castelli D.D., Viale A., Aime S. Challenges for molecular magnetic resonance imaging. Chemical Reviews 2010, 110:3019-3042.
382. van Rijt S.H., Sadler P.J. Current applications and future potential for bioinorganic chemistry in the development of anticancer drugs. Drug Discovery Today 2009, 14:1089-1097.
383. WHO (2004). Assessing the iron status of populations. Report of a joint World Health Organisation/Centers for Disease Control and Prevention technical consultation.
384. Dietz R., Outridge P.M., Hobson K.A. Anthropogenic contributions to mercury levels in present-day Arctic animals-a review. Science of the Total Environment 2009, 407:6120-6131.
385. Emsley J. Molecules of murder. Criminal molecules and classic cases 2008, RSC Publishing.
386. Guzzi G., La Porta C.A. Molecular mechanisms triggered by mercury. Toxicology 2008, 244:1-12.
387. Jaffe E.K., Martins J., Li J., Kervinen J., Dunbrack R.L. The molecular mechanism of lead inhibition of human porphobilinogen synthase. Journal of Biological Chemistry 2001, 276:1531-1537.
388. 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.
389. Martin R.B. Aluminium: A Neurotoxic Product of Acid Rain. Acc Chem Res 1994, 27:204-210.
390. Prince R.C., Gailer J., Gunson D.E., Turner R.J., George G.N., Pickering I.J. Strong poison revisited. Journal of Inorganic Biochemistry 2007, 101:1891-1893.
391. Ralston N.V., Raymond L.J. Dietary selenium's protective effects against methylmercury toxicity. Toxicology 2010, 278:112-123.
392. Verstraeten S.V., Aimo L., Oteiza P.I. Aluminium and lead: molecular mechanisms of brain toxicity. Archives of Toxicology 2008, 82:789-802.