60
M. Stein
Carefully and accurately performed quantum chemical calculations of EPR
parameters must not only try to reproduce g- and hyperfine tensor principal values
but also consider information about their absolute and relative orientations. Despite
recent progress in treating spin–orbit coupling and electron correlation appropriately,
more basic research and development of methods for transition metal containing systems is required to provide reliable answers for complex systems from chemistry and
biology.
Acknowledgements Support by the Max Planck Society for the Advancement of Science is
acknowledged. Part of this work was also financed by the EU COST Action CM1305 ‘ECOSTBio’
and the EU-program ERDF (European Regional Development Fund) of the German Federal State
Saxony-Anhalt within the Research Center of Dynamic Systems (CDS).
References
1. Abragam A, Bleaney B (1970) Electron paramagnetic resonance of transition ions. Oxford
University Press, Oxford
2. Mabbs FE, Collinson D (1992) Electron paramagnetic resonance of d transition metal compounds. Elsevier, Amsterdam
3. Boer JL, Mulrooney SB, Hausinger RP (2014) Nickel-dependent metalloenzymes. Arch
Biochem Biophys 0:142–152
4. Walsh CT, Orme-Johnson WH (1987) Nickel enzymes. Biochemistry 26:4901–4906
5. Lubitz W, Ogata H, Rudiger O, Reijerse E (2014) Hydrogenases. Chem Rev 114:4081–4148
6. Lubitz W, Reijerse E, van Gastel M (2007) NiFe and FeFe hydrogenases studied by advanced
magnetic resonance techniques. Chem Rev 107:4331–4365
7. Siegbahn PEM, Tye JW, Hall MB (2007) Computational studies of NiFe and FeFe hydrogenases. Chem Rev 107:4414–4435
8. Stein M, Lubitz W (2002) Quantum chemical calculations of NiFe hydrogenase. Curr Opin
Chem Biol 6:243–249
9. Hille R (2002) Molybdenum and tungsten in biology. Trends Biochem Sci 27:360–367
10. Igarashi RY, Seefeldt LC (2003) Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Crit Rev Biochem Mol Biol 38:351–384
11. Metz S, Thiel W (2011) Theoretical studies on the reactivity of molybdenum enzymes. Coord
Chem Rev 255:1085–1103
12. Richards RL (1996) Reactions of small molecules at transition metal sites: studies relevant to
nitrogenase, an organometallic enzyme. Coord Chem Rev 154:83–97
13. Kisker C, Schindelin H, Rees DC (1997) Molybdenum-cofactor-containing enzymes: structure
and mechanism. Annu Rev Biochem 66:233–267
14. Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96:2757–2816
15. Zelko IN, Mariani TJ, Folz RJ (2002) Superoxide dismutase multigene family: a comparison of
the CuZn–SOD (SOD1), Mn–SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution,
and expression. Free Radic Biol Med 33:337–349
16. Nordberg J, Arner ESJ (2001) Reactive oxygen species, antioxidants, and the mammalian
thioredoxin system. Free Radic Biol Med 31:1287–1312
17. Dismukes GC, Brimblecombe R, Felton GAN, Pryadun RS, Sheats JE, Spiccia L, Swiegers GF
(2009) Development of bioinspired Mn4O4-Cubane water oxidation catalysts: lessons from
photosynthesis. Acc Chem Res 42:1935–1943
18. Barber J (2006) Photosystem II: an enzyme of global significance. Biochem Soc Trans
34:619–631
M. Stein
Carefully and accurately performed quantum chemical calculations of EPR
parameters must not only try to reproduce g- and hyperfine tensor principal values
but also consider information about their absolute and relative orientations. Despite
recent progress in treating spin–orbit coupling and electron correlation appropriately,
more basic research and development of methods for transition metal containing systems is required to provide reliable answers for complex systems from chemistry and
biology.
Acknowledgements Support by the Max Planck Society for the Advancement of Science is
acknowledged. Part of this work was also financed by the EU COST Action CM1305 ‘ECOSTBio’
and the EU-program ERDF (European Regional Development Fund) of the German Federal State
Saxony-Anhalt within the Research Center of Dynamic Systems (CDS).
References
1. Abragam A, Bleaney B (1970) Electron paramagnetic resonance of transition ions. Oxford
University Press, Oxford
2. Mabbs FE, Collinson D (1992) Electron paramagnetic resonance of d transition metal compounds. Elsevier, Amsterdam
3. Boer JL, Mulrooney SB, Hausinger RP (2014) Nickel-dependent metalloenzymes. Arch
Biochem Biophys 0:142–152
4. Walsh CT, Orme-Johnson WH (1987) Nickel enzymes. Biochemistry 26:4901–4906
5. Lubitz W, Ogata H, Rudiger O, Reijerse E (2014) Hydrogenases. Chem Rev 114:4081–4148
6. Lubitz W, Reijerse E, van Gastel M (2007) NiFe and FeFe hydrogenases studied by advanced
magnetic resonance techniques. Chem Rev 107:4331–4365
7. Siegbahn PEM, Tye JW, Hall MB (2007) Computational studies of NiFe and FeFe hydrogenases. Chem Rev 107:4414–4435
8. Stein M, Lubitz W (2002) Quantum chemical calculations of NiFe hydrogenase. Curr Opin
Chem Biol 6:243–249
9. Hille R (2002) Molybdenum and tungsten in biology. Trends Biochem Sci 27:360–367
10. Igarashi RY, Seefeldt LC (2003) Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Crit Rev Biochem Mol Biol 38:351–384
11. Metz S, Thiel W (2011) Theoretical studies on the reactivity of molybdenum enzymes. Coord
Chem Rev 255:1085–1103
12. Richards RL (1996) Reactions of small molecules at transition metal sites: studies relevant to
nitrogenase, an organometallic enzyme. Coord Chem Rev 154:83–97
13. Kisker C, Schindelin H, Rees DC (1997) Molybdenum-cofactor-containing enzymes: structure
and mechanism. Annu Rev Biochem 66:233–267
14. Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96:2757–2816
15. Zelko IN, Mariani TJ, Folz RJ (2002) Superoxide dismutase multigene family: a comparison of
the CuZn–SOD (SOD1), Mn–SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution,
and expression. Free Radic Biol Med 33:337–349
16. Nordberg J, Arner ESJ (2001) Reactive oxygen species, antioxidants, and the mammalian
thioredoxin system. Free Radic Biol Med 31:1287–1312
17. Dismukes GC, Brimblecombe R, Felton GAN, Pryadun RS, Sheats JE, Spiccia L, Swiegers GF
(2009) Development of bioinspired Mn4O4-Cubane water oxidation catalysts: lessons from
photosynthesis. Acc Chem Res 42:1935–1943
18. Barber J (2006) Photosystem II: an enzyme of global significance. Biochem Soc Trans
34:619–631