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2
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0242695597
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The active site and catalytic mechanism of NiFe hydrogenases
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Volbeda A, Fontecilla-Camps JC: The active site and catalytic mechanism of NiFe hydrogenases, Dalton Transactions 2003:4030-4038.
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Dalton Transactions
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Volbeda, A.1
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3
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0142244261
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Chemistry and the hydrogenases
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This provides a chemists' view of the structures of NiFe and Fe-only catalytic sites and the progress being made in synthesising small complexes that model structures or activities.
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Evans D.J., Pickett C.J. Chemistry and the hydrogenases. Chem Soc Rev. 32:2003;268-275 This provides a chemists' view of the structures of NiFe and Fe-only catalytic sites and the progress being made in synthesising small complexes that model structures or activities.
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Chem Soc Rev
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, pp. 268-275
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Evans, D.J.1
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4
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0037386540
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The organometallic active site of [Fe]hydrogenase: Models and entatic states
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This article discusses the significance of the iron carbonyl thiolate site from the earliest stages of biological evolution to contemporary chemical principles.
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Darensbourg M.Y., Lyon E.J., Zhao X., Georgakaki I.P. The organometallic active site of [Fe]hydrogenase: models and entatic states. Proc Natl Acad Sci USA. 100:2003;3683-3688 This article discusses the significance of the iron carbonyl thiolate site from the earliest stages of biological evolution to contemporary chemical principles.
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Proc Natl Acad Sci USA
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Darensbourg, M.Y.1
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0036618091
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Hydrogenases in green algae: Do they save the algae's life and solve our energy problems?
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Happe T., Hemschemeier A., Winkler M., Kaminski A. Hydrogenases in green algae: do they save the algae's life and solve our energy problems? Trends Plant Sci. 7:2002;246-250.
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Trends Plant Sci
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Happe, T.1
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7
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0036093965
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Hydrogen fuel electrode based on bioelectrocatalysis by the enzyme hydrogenase
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Karyakin A.A., Morozov S.V., Karyakina E.E., Varfolomeyev S.D., Zorin N.A., Cosnier S. Hydrogen fuel electrode based on bioelectrocatalysis by the enzyme hydrogenase. Electrochem Commun. 4:2002;417-420.
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Electrochem Commun
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Karyakin, A.A.1
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Varfolomeyev, S.D.4
Zorin, N.A.5
Cosnier, S.6
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8
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0037149937
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Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
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Jones AK, Sillery E, Albracht SPJ, Armstrong FA: Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun 2002:866-867.
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Chem Commun
, pp. 866-867
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Jones, A.K.1
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Albracht, S.P.J.3
Armstrong, F.A.4
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9
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0036836422
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High-resolution crystallographic analysis of Desulfovibrio fructosovorans [NiFe] hydrogenase
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Volbeda A., Montet Y., Vernède X., Hatchikian E.C., Fontecilla-Camps J.C. High-resolution crystallographic analysis of Desulfovibrio fructosovorans [NiFe] hydrogenase. Int J Hydrogen Energy. 27:2002;1449-1461.
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Volbeda, A.1
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Hatchikian, E.C.4
Fontecilla-Camps, J.C.5
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11
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0035961483
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Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
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Nicolet Y., De Lacey A.L., Vernède X., Fernandez V.M., Hatchikian E.C., Fontecilla-Camps J.C. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J Am Chem Soc. 123:2001;1596-1601.
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Nicolet, Y.1
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Fontecilla-Camps, J.C.6
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12
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0037009993
-
Structural studies of the carbon monoxide complex of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the initial activation site for dihydrogen
-
This presents the first crystallographic evidence that exogenous CO binds to the Ni atom of the NiFe active site.
-
Ogata H., Mizoguchi Y., Mizuno N., Miki K., Adachi S., Yasuoka N., Yagi T., Yamauchi O., Hirota S., Higuchi Y. Structural studies of the carbon monoxide complex of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the initial activation site for dihydrogen. J Am Chem Soc. 124:2002;11628-11635 This presents the first crystallographic evidence that exogenous CO binds to the Ni atom of the NiFe active site.
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J Am Chem Soc
, vol.124
, pp. 11628-11635
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Ogata, H.1
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Yagi, T.7
Yamauchi, O.8
Hirota, S.9
Higuchi, Y.10
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13
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0036932958
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IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase
-
This describes infrared data and DFT calculations showing that exogenous CO is weakly bound to the Ni atom of the NiFe active site.
-
De Lacey A.L., Stadler C., Fernandez V.N., Hatchikian E.C., Fan H.J., Li S., Hall M.B. IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase. J Biol Inorg Chem. 7:2002;318-326 This describes infrared data and DFT calculations showing that exogenous CO is weakly bound to the Ni atom of the NiFe active site.
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J Biol Inorg Chem
, vol.7
, pp. 318-326
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De Lacey, A.L.1
Stadler, C.2
Fernandez, V.N.3
Hatchikian, E.C.4
Fan, H.J.5
Li, S.6
Hall, M.B.7
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14
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0037065697
-
Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: Examination of its light sensitivity at cryogenic temperatures
-
This reports the first infrared spectra to be obtained for oxidised and CO-inhibited forms of Clostridium pasteurianum Fe-only hydrogenase. It also presents infrared evidence for facile interconversions between active site forms with and without a bridging CO ligand.
-
Chen Z., Lemon B.J., Huang S., Swartz D.J., Peters J.W., Bagley K.A. Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: examination of its light sensitivity at cryogenic temperatures. Biochemistry. 41:2002;2036-2043 This reports the first infrared spectra to be obtained for oxidised and CO-inhibited forms of Clostridium pasteurianum Fe-only hydrogenase. It also presents infrared evidence for facile interconversions between active site forms with and without a bridging CO ligand.
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Biochemistry
, vol.41
, pp. 2036-2043
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Chen, Z.1
Lemon, B.J.2
Huang, S.3
Swartz, D.J.4
Peters, J.W.5
Bagley, K.A.6
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15
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0037178939
-
Density functional claculations for modeling the active site of nickel-iron hydrogenases. 2. Predictions for the unready and ready states and the corresponding activation processes
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This proposes a model in which the difference between Ni-A and Ni-B lies in the orientation of a nearby glutamate side-chain.
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Stadler C., De Lacey A.L., Montet Y., Volbeda A., Fontecilla-Camps J.C., Conesa J.C., Fernandez V.M. Density functional claculations for modeling the active site of nickel-iron hydrogenases. 2. Predictions for the unready and ready states and the corresponding activation processes. Inorg Chem. 41:2002;4424-4434 This proposes a model in which the difference between Ni-A and Ni-B lies in the orientation of a nearby glutamate side-chain.
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Inorg Chem
, vol.41
, pp. 4424-4434
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Stadler, C.1
De Lacey, A.L.2
Montet, Y.3
Volbeda, A.4
Fontecilla-Camps, J.C.5
Conesa, J.C.6
Fernandez, V.M.7
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16
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0033611949
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Theoretical characterization of the reaction intermediates in a model of the nickel-iron hydrogenase of Desulfovibrio gigas
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Niu S., Thomson L.M., Hall M.B. Theoretical characterization of the reaction intermediates in a model of the nickel-iron hydrogenase of Desulfovibrio gigas. J Am Chem Soc. 121:1999;4000-4007.
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Niu, S.1
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0034846069
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Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism
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Maroney M.J., Bryngelson P. Spectroscopic and model studies of the Ni-Fe hydrogenase reaction mechanism. J Biol Inorg Chem. 6:2001;453-459.
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J Biol Inorg Chem
, vol.6
, pp. 453-459
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Maroney, M.J.1
Bryngelson, P.2
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19
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0034851266
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Recent theoretical predictions of the active site for the observed forms in the catalytic cycle of Ni-Fe hydrogenase
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Fan H-J., Hall M.B. Recent theoretical predictions of the active site for the observed forms in the catalytic cycle of Ni-Fe hydrogenase. J Biol Inorg Chem. 6:2001;467-473.
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J Biol Inorg Chem
, vol.6
, pp. 467-473
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Fan, H.-J.1
Hall, M.B.2
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20
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0036525727
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Quantum chemical calculations of [NiFe] hydrogenase
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This recent Current Opinion appraises the theoretical investigations of NiFe active site structures and mechanistic proposals, focusing mainly on the literature appearing in 2001.
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Stein M., Lubitz W. Quantum chemical calculations of [NiFe] hydrogenase. Curr Opin Chem Biol. 6:2002;243-249 This recent Current Opinion appraises the theoretical investigations of NiFe active site structures and mechanistic proposals, focusing mainly on the literature appearing in 2001.
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Curr Opin Chem Biol
, vol.6
, pp. 243-249
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Stein, M.1
Lubitz, W.2
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21
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0037160427
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High-spin Ni(II), a surprisingly good structural model for [NiFe] hydrogenase
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Fan H-J., Hall M.B. High-spin Ni(II), a surprisingly good structural model for [NiFe] hydrogenase. J Am Chem Soc. 124:2002;394-395.
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J Am Chem Soc
, vol.124
, pp. 394-395
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Fan, H.-J.1
Hall, M.B.2
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22
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0037248819
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Refinement of the nickel site structure in Desulfovibrio gigas hydrogenase using range-extended EXAFS spectroscopy
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Gu W., Jacquamet L., Patil D.S., Wang H-X., Evans D.J., Smith M.C., Millar M., Koch S., Eichhorn D.M., Latimer M., Cramer S.P. Refinement of the nickel site structure in Desulfovibrio gigas hydrogenase using range-extended EXAFS spectroscopy. J Inorg Biochem. 93:2003;41-51.
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J Inorg Biochem
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, pp. 41-51
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Gu, W.1
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Koch, S.8
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23
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0141812899
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The assembly line
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Edited by Cammack R, Frey M, Robson, R. London and New York: Taylor and Francis;
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Robson R: The assembly line. In Hydrogen as a Fuel; Learning from Nature. Edited by Cammack R, Frey M, Robson, R. London and New York: Taylor and Francis; 2001: 57-72.
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Hydrogen as a Fuel; Learning from Nature
, pp. 57-72
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Robson, R.1
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24
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0036671203
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Metal insertion into NiFe hydrogenases
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Blokesch M., Paschos A., Theodoratou E., Bauer A., Hube M., Huth S., Böck A. Metal insertion into NiFe hydrogenases. Biochem Soc Trans. 30:2002;674-680.
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Biochem Soc Trans
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, pp. 674-680
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Blokesch, M.1
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Böck, A.7
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25
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0346890205
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Taming of a poison: Biosynthesis of the NiFe-hydrogenase cyanide ligands
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Reissmann S., Hochleitner E., Wang H., Paschos A., Lottspeich F., Glass R.S., Böck A. Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands. Science. 299:2003;1067-1070.
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Science
, vol.299
, pp. 1067-1070
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Reissmann, S.1
Hochleitner, E.2
Wang, H.3
Paschos, A.4
Lottspeich, F.5
Glass, R.S.6
Böck, A.7
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26
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1842578056
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Regulation of hydrogenase gene expression
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Edited by Cammack R, Frey M, Robson, R. London and New York: Taylor and Francis;
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Friedrich B, Vignais PM, Lenz O, Colbeau A: Regulation of hydrogenase gene expression. In Hydrogen as a Fuel; Learning from Nature. Edited by Cammack R, Frey M, Robson, R. London and New York: Taylor and Francis; 2001: 33-56.
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, pp. 33-56
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Friedrich, B.1
Vignais, P.M.2
Lenz, O.3
Colbeau, A.4
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0037044954
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2 metabolism on Fe-only hydrogenases
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2 metabolism on Fe-only hydrogenases. J Chem Phys. 117:2002;8177-8180.
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J Chem Phys
, vol.117
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Liu, Z.-P.1
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28
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0037042289
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A density functional theory study on the active center of Fe-only hydrogenase: Characterization and electronic structure of the redox states
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2, and the redox-state selective inhibition by CO.
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2, and the redox-state selective inhibition by CO.
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J Am Chem Soc
, vol.124
, pp. 5175-5182
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Liu, Z.-P.1
Hu, P.2
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30
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0037622847
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H subcluster
-
2 cleavage may involve both distal and proximal Fe atoms, and a bridging hydride might be formed.
-
2 cleavage may involve both distal and proximal Fe atoms, and a bridging hydride might be formed.
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Inorg Chem
, vol.42
, pp. 4773-4781
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Bruschi, M.1
Fantucci, P.2
De Gioia, L.3
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31
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0038001623
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Probing the electronic structure of the diiron subsite of [Fe]-hydrogenase: A photoelectron spectroscopic study of Fe(I)-Fe(I) model complexes
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Yang X., Razavet M., Wang X-B., Pickett C.J., Wang L-S. Probing the electronic structure of the diiron subsite of [Fe]-hydrogenase: a photoelectron spectroscopic study of Fe(I)-Fe(I) model complexes. J Phys Chem A. 107:2003;4612-4618.
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J Phys Chem a
, vol.107
, pp. 4612-4618
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Yang, X.1
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0041508447
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2-: Implications with respect to hydrogenases
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2-: implications with respect to hydrogenases. Inorg Chem. 42:2003;5046-5048.
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Inorg Chem
, vol.42
, pp. 5046-5048
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Kayal, A.1
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0035175063
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The [NiFe] hydrogenase from Allochromatium vinosum studied in EPR-detectable states: H/D exchange experiments that yield new information about the structure of the active site
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Bleijlevens B., Faber B.W., Albracht S.P.J. The [NiFe] hydrogenase from Allochromatium vinosum studied in EPR-detectable states: H/D exchange experiments that yield new information about the structure of the active site. J Biol Inorg Chem. 6:2001;763-769.
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J Biol Inorg Chem
, vol.6
, pp. 763-769
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Bleijlevens, B.1
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Albracht, S.P.J.3
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37
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0142152415
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2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy
-
2-sensing enzyme gives a Ni-C EPR spectrum that is not complicated by the reduced proximal [4Fe-4S] cluster. ENDOR and ESEEM experiments provide direct evidence for a hydride ligand occupying a bridging position.
-
2-sensing enzyme gives a Ni-C EPR spectrum that is not complicated by the reduced proximal [4Fe-4S] cluster. ENDOR and ESEEM experiments provide direct evidence for a hydride ligand occupying a bridging position.
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J Am Chem Soc
, vol.125
, pp. 13075-13083
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Brecht, M.1
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38
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1842578061
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EPR and ENDOR studies of [NiFe] hydrogenase: Contributions to understanding the mechanism of biological hydrogen conversion
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A good account of recent spectroscopic investigations of NiFe hydrogenases.
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Lubitz W., Brecht M., Foerster S., van Gastel M., Stein M. EPR and ENDOR studies of [NiFe] hydrogenase: contributions to understanding the mechanism of biological hydrogen conversion. ACS Symp Ser. 858:2003;128-149 A good account of recent spectroscopic investigations of NiFe hydrogenases.
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ACS Symp Ser
, vol.858
, pp. 128-149
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Lubitz, W.1
Brecht, M.2
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Stein, M.5
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39
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0037425515
-
Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfiovibrio vulgaris Miyazaki F
-
This paper provides important spectroscopic and DFT support for a hydride ligand at a bridging position in Ni-C and its removal when the enzyme is illuminated at low temperature to give Ni-L.
-
Foerster S., Stein M., Brecht M., Ogata H., Higuchi Y., Lubitz W. Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfiovibrio vulgaris Miyazaki F. J Am Chem Soc. 125:2003;83-93 This paper provides important spectroscopic and DFT support for a hydride ligand at a bridging position in Ni-C and its removal when the enzyme is illuminated at low temperature to give Ni-L.
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J Am Chem Soc
, vol.125
, pp. 83-93
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Foerster, S.1
Stein, M.2
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40
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0037257457
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Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovorans Ni-Fe hydrogenase
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De Lacey A.L., Fernandez V.M., Rousset M., Cavazza C., Hatchikian E.C. Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovorans Ni-Fe hydrogenase. J Biol Inorg Chem. 8:2003;129-134.
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J Biol Inorg Chem
, vol.8
, pp. 129-134
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De Lacey, A.L.1
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0037207118
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Enzyme electrokinetics: Hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase
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Léger C, Jones AK, Roseboom W, Albracht SPJ, Armstrong FA: Enzyme electrokinetics: Hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase. Biochemistry 2002, 41:15736-15746.
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Biochemistry
, vol.41
, pp. 15736-15746
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42
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Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes
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Léger C., Jones A.K., Albracht S.P.J., Armstrong F.A. Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes. J Phys Chem B. 106:2002;13058-13063.
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0038375489
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Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase
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Jones AK, Lamle SE, Pershad HR, Vincent KA, Albracht SPJ, Armstrong FA: Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. J Am Chem Soc 2003, 125:8505-8514.
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J Am Chem Soc
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Jones, A.K.1
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Hydrogenase on an electrode: A remarkable heterogeneous catalyst
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Lamle SE, Vincent KA, Halliwell LM, Albracht SPJ, Armstrong FA: Hydrogenase on an electrode: a remarkable heterogeneous catalyst. Dalton Transactions 2003:4152-4157.
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Dalton Transactions
, pp. 4152-4157
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Lamle, S.E.1
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Laurinavichene T.V., Zorin N.A., Tsygankov A.A. Effect of redox potential on activity of hydrogenase 1 and hydrogenase 2 in Escherichia coli. Arch Microbiol. 178:2002;437-442.
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Laurinavichene, T.V.1
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Tsygankov, A.A.3
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46
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0037116445
-
x)-Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas
-
This paper provides new evidence on the nature of the oxide/hydroxide ligand in Ni-A, suggesting that it is derived from a solvent water molecule.
-
x)-Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas J Am Chem Soc. 124:2002;281-286 This paper provides new evidence on the nature of the oxide/hydroxide ligand in Ni-A, suggesting that it is derived from a solvent water molecule.
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J Am Chem Soc
, vol.124
, pp. 281-286
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Carepo, M.1
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