메뉴 건너뛰기




Volumn 7, Issue 16, 2016, Pages 3290-3293

Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; INFRARED SPECTROSCOPY;

EID: 84983261297     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/acs.jpclett.6b01316     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 0036523377 scopus 로고    scopus 로고
    • Hydrogenases: Hydrogen-Activating Enzymes
    • Frey, M. Hydrogenases: Hydrogen-Activating Enzymes ChemBioChem 2002, 3, 153-160 10.1002/1439-7633(20020301)3:2/3<153::AID-CBIC153>3.0.CO;2-B
    • (2002) ChemBioChem , vol.3 , pp. 153-160
    • Frey, M.1
  • 4
    • 35748930865 scopus 로고    scopus 로고
    • Structure/Function Relationships of [NiFe]-and [FeFe]-hydrogenases
    • Fontecilla-Camps, J. C.; Volbeda, A.; Cavazza, C.; Nicolet, Y. Structure/Function Relationships of [NiFe]-and [FeFe]-hydrogenases Chem. Rev. 2007, 107, 4273-4303 10.1021/cr050195z
    • (2007) Chem. Rev. , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 5
    • 67649283572 scopus 로고    scopus 로고
    • Structural and Functional Analogues of the Active Sites of the [Fe]-,[NiFe]-, and [FeFe]-hydrogenases
    • Tard, C.; Pickett, C. J. Structural and Functional Analogues of the Active Sites of the [Fe]-,[NiFe]-, and [FeFe]-hydrogenases Chem. Rev. 2009, 109, 2245-2274 10.1021/cr800542q
    • (2009) Chem. Rev. , vol.109 , pp. 2245-2274
    • Tard, C.1    Pickett, C.J.2
  • 6
    • 35748942883 scopus 로고    scopus 로고
    • Computational Studies of [NiFe] and [FeFe] Hydrogenases
    • Siegbahn, P. E.; Tye, J. W.; Hall, M. B. Computational Studies of [NiFe] and [FeFe] Hydrogenases Chem. Rev. 2007, 107, 4414-4435 10.1021/cr050185y
    • (2007) Chem. Rev. , vol.107 , pp. 4414-4435
    • Siegbahn, P.E.1    Tye, J.W.2    Hall, M.B.3
  • 7
    • 84860374319 scopus 로고    scopus 로고
    • Recent Progress in Electrochemical Hydrogen Production with Earth-Abundant Metal Complexes as Catalysts
    • Wang, M.; Chen, L.; Sun, L. Recent Progress in Electrochemical Hydrogen Production with Earth-Abundant Metal Complexes as Catalysts Energy Environ. Sci. 2012, 5, 6763-6778 10.1039/c2ee03309g
    • (2012) Energy Environ. Sci. , vol.5 , pp. 6763-6778
    • Wang, M.1    Chen, L.2    Sun, L.3
  • 9
    • 83655183063 scopus 로고    scopus 로고
    • Combining Acid-Base, Redox and Substrate Binding Functionalities to Give a Complete Model for the [FeFe]-Hydrogenase
    • Camara, J. M.; Rauchfuss, T. B. Combining Acid-Base, Redox and Substrate Binding Functionalities to Give a Complete Model for the [FeFe]-Hydrogenase Nat. Chem. 2011, 4, 26-30 10.1038/nchem.1180
    • (2011) Nat. Chem. , vol.4 , pp. 26-30
    • Camara, J.M.1    Rauchfuss, T.B.2
  • 10
    • 84887769490 scopus 로고    scopus 로고
    • Enhanced Photochemical Hydrogen Production by a Molecular Diiron Catalyst Incorporated into a Metal-Organic Framework
    • Pullen, S.; Fei, H.; Orthaber, A.; Cohen, S. M.; Ott, S. Enhanced Photochemical Hydrogen Production by a Molecular Diiron Catalyst Incorporated into a Metal-Organic Framework J. Am. Chem. Soc. 2013, 135, 16997-17003 10.1021/ja407176p
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16997-17003
    • Pullen, S.1    Fei, H.2    Orthaber, A.3    Cohen, S.M.4    Ott, S.5
  • 12
    • 84859119897 scopus 로고    scopus 로고
    • Characterization of Photochemical Processes for H2 Production by CdS Nanorod-[FeFe] Hydrogenase Complexes
    • Brown, K. A.; Wilker, M. B.; Boehm, M.; Dukovic, G.; King, P. W. Characterization of Photochemical Processes for H2 Production by CdS Nanorod-[FeFe] Hydrogenase Complexes J. Am. Chem. Soc. 2012, 134, 5627-5636 10.1021/ja2116348
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5627-5636
    • Brown, K.A.1    Wilker, M.B.2    Boehm, M.3    Dukovic, G.4    King, P.W.5
  • 13
    • 78349259311 scopus 로고    scopus 로고
    • Controlled Assembly of Hydrogenase-CdTe Nanocrystal Hybrids for Solar Hydrogen Production
    • Brown, K. A.; Dayal, S.; Ai, X.; Rumbles, G.; King, P. W. Controlled Assembly of Hydrogenase-CdTe Nanocrystal Hybrids for Solar Hydrogen Production J. Am. Chem. Soc. 2010, 132, 9672-9680 10.1021/ja101031r
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9672-9680
    • Brown, K.A.1    Dayal, S.2    Ai, X.3    Rumbles, G.4    King, P.W.5
  • 14
    • 84863229565 scopus 로고    scopus 로고
    • Artificial Photosynthetic Systems Based on [FeFe]-Hydrogenase Mimics: The Road to High Efficiency for Light-Driven Hydrogen Evolution
    • Wang, F.; Wang, W.-G.; Wang, H.-Y.; Si, G.; Tung, C.-H.; Wu, L.-Z. Artificial Photosynthetic Systems Based on [FeFe]-Hydrogenase Mimics: the Road to High Efficiency for Light-Driven Hydrogen Evolution ACS Catal. 2012, 2, 407-416 10.1021/cs200458b
    • (2012) ACS Catal. , vol.2 , pp. 407-416
    • Wang, F.1    Wang, W.-G.2    Wang, H.-Y.3    Si, G.4    Tung, C.-H.5    Wu, L.-Z.6
  • 15
    • 78650856943 scopus 로고    scopus 로고
    • Wiring an [FeFe]-Hydrogenase with Photosystem i for Light-Induced Hydrogen Production
    • Lubner, C. E.; Knörzer, P.; Silva, P. J.; Vincent, K. A.; Happe, T.; Bryant, D. A.; Golbeck, J. H. Wiring an [FeFe]-Hydrogenase with Photosystem I for Light-Induced Hydrogen Production Biochemistry 2010, 49, 10264-10266 10.1021/bi1016167
    • (2010) Biochemistry , vol.49 , pp. 10264-10266
    • Lubner, C.E.1    Knörzer, P.2    Silva, P.J.3    Vincent, K.A.4    Happe, T.5    Bryant, D.A.6    Golbeck, J.H.7
  • 16
    • 33750337726 scopus 로고    scopus 로고
    • Photosynthesis as a Power Supply for (Bio-) Hydrogen Production
    • Esper, B.; Badura, A.; Rögner, M. Photosynthesis as a Power Supply for (Bio-) Hydrogen Production Trends Plant Sci. 2006, 11, 543-549 10.1016/j.tplants.2006.09.001
    • (2006) Trends Plant Sci. , vol.11 , pp. 543-549
    • Esper, B.1    Badura, A.2    Rögner, M.3
  • 17
    • 84969834501 scopus 로고    scopus 로고
    • Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry
    • Armstrong, F. A.; Evans, R. M.; Hexter, S. V.; Murphy, B. J.; Roessler, M. M.; Wulff, P. Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry Acc. Chem. Res. 2016, 49, 884-892 10.1021/acs.accounts.6b00027
    • (2016) Acc. Chem. Res. , vol.49 , pp. 884-892
    • Armstrong, F.A.1    Evans, R.M.2    Hexter, S.V.3    Murphy, B.J.4    Roessler, M.M.5    Wulff, P.6
  • 18
    • 84955442631 scopus 로고    scopus 로고
    • Detection of Transient Intermediates Generated from Subsite Analogues of [FeFe] Hydrogenases
    • Hunt, N. T.; Wright, J. A.; Pickett, C. Detection of Transient Intermediates Generated from Subsite Analogues of [FeFe] Hydrogenases Inorg. Chem. 2016, 55, 399-410 10.1021/acs.inorgchem.5b02477
    • (2016) Inorg. Chem. , vol.55 , pp. 399-410
    • Hunt, N.T.1    Wright, J.A.2    Pickett, C.3
  • 19
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and Exploiting the Electrocatalytic Properties of Hydrogenases
    • Vincent, K. A.; Parkin, A.; Armstrong, F. A. Investigating and Exploiting the Electrocatalytic Properties of Hydrogenases Chem. Rev. 2007, 107, 4366-4413 10.1021/cr050191u
    • (2007) Chem. Rev. , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 20
    • 0037065697 scopus 로고    scopus 로고
    • Infrared Studies of the CO-Inhibited Form of the Fe-Only Hydrogenase from Clostridium pasteurianum I: Examination of its Light Sensitivity at Cryogenic Temperatures
    • 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 2002, 41, 2036-2043 10.1021/bi011510o
    • (2002) Biochemistry , vol.41 , pp. 2036-2043
    • Chen, Z.1    Lemon, B.J.2    Huang, S.3    Swartz, D.J.4    Peters, J.W.5    Bagley, K.A.6
  • 24
    • 84868533696 scopus 로고    scopus 로고
    • Identification and Characterization of the "super-Reduced" State of the H-Cluster in [FeFe] Hydrogenase: A New Building Block for the Catalytic Cycle?
    • Adamska, A.; Silakov, A.; Lambertz, C.; Rüdiger, O.; Happe, T.; Reijerse, E.; Lubitz, W. Identification and Characterization of the "Super-Reduced" State of the H-Cluster in [FeFe] Hydrogenase: A New Building Block for the Catalytic Cycle? Angew. Chem., Int. Ed. 2012, 51, 11458-11462 10.1002/anie.201204800
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 11458-11462
    • Adamska, A.1    Silakov, A.2    Lambertz, C.3    Rüdiger, O.4    Happe, T.5    Reijerse, E.6    Lubitz, W.7
  • 26
    • 33845932878 scopus 로고    scopus 로고
    • Electrochemical Investigations of the Interconversions between Catalytic and Inhibited States of the [FeFe]-Hydrogenase from Desulfovibrio desulfuricans
    • Parkin, A.; Cavazza, C.; Fontecilla-Camps, J. C.; Armstrong, F. A. Electrochemical Investigations of the Interconversions between Catalytic and Inhibited States of the [FeFe]-Hydrogenase from Desulfovibrio desulfuricans J. Am. Chem. Soc. 2006, 128, 16808-16815 10.1021/ja064425i
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16808-16815
    • Parkin, A.1    Cavazza, C.2    Fontecilla-Camps, J.C.3    Armstrong, F.A.4
  • 27
    • 70350234815 scopus 로고    scopus 로고
    • Electrochemical Kinetic Investigations of the Reactions of [FeFe]-Hydrogenases with Carbon Monoxide and Oxygen: Comparing the Importance of Gas Tunnels and Active-Site Electronic/Redox Effects
    • Goldet, G.; Brandmayr, C.; Stripp, S. T.; Happe, T.; Cavazza, C.; Fontecilla-Camps, J. C.; Armstrong, F. A. Electrochemical Kinetic Investigations of the Reactions of [FeFe]-Hydrogenases with Carbon Monoxide and Oxygen: Comparing the Importance of Gas Tunnels and Active-Site Electronic/Redox Effects J. Am. Chem. Soc. 2009, 131, 14979-14989 10.1021/ja905388j
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14979-14989
    • Goldet, G.1    Brandmayr, C.2    Stripp, S.T.3    Happe, T.4    Cavazza, C.5    Fontecilla-Camps, J.C.6    Armstrong, F.A.7
  • 30
    • 70149086048 scopus 로고    scopus 로고
    • Direct Observation of Ligand Dynamics in Cytochrome c
    • Thielges, M. C.; Zimmermann, J.; Romesberg, F. E. Direct Observation of Ligand Dynamics in Cytochrome c J. Am. Chem. Soc. 2009, 131, 6054-6055 10.1021/ja810155s
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6054-6055
    • Thielges, M.C.1    Zimmermann, J.2    Romesberg, F.E.3
  • 31
    • 0000884183 scopus 로고
    • Time-Resolved FT-IR Absorption Spectroscopy Using a Step-Scan Interferometer
    • Uhmann, W.; Becker, A.; Taran, C.; Siebert, F. Time-Resolved FT-IR Absorption Spectroscopy Using a Step-Scan Interferometer Appl. Spectrosc. 1991, 45, 390-397 10.1366/0003702914337128
    • (1991) Appl. Spectrosc. , vol.45 , pp. 390-397
    • Uhmann, W.1    Becker, A.2    Taran, C.3    Siebert, F.4
  • 32
    • 84926631905 scopus 로고    scopus 로고
    • Proton-Coupled Electron Transfer Dynamics in the Catalytic Mechanism of a [NiFe]-Hydrogenase
    • Greene, B. L.; Wu, C.-H.; McTernan, P. M.; Adams, M. W. W.; Dyer, R. B. Proton-Coupled Electron Transfer Dynamics in the Catalytic Mechanism of a [NiFe]-Hydrogenase J. Am. Chem. Soc. 2015, 137, 4558-4566 10.1021/jacs.5b01791
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 4558-4566
    • Greene, B.L.1    Wu, C.-H.2    McTernan, P.M.3    Adams, M.W.W.4    Dyer, R.B.5
  • 34
    • 0021111948 scopus 로고
    • Geminate Recombination of Carbon Monoxide to Myoglobin
    • Henry, E. R.; Sommer, J. H.; Hofrichter, J.; Eaton, W. A.; Gellert, M. Geminate Recombination of Carbon Monoxide to Myoglobin J. Mol. Biol. 1983, 166, 443-451 10.1016/S0022-2836(83)80094-1
    • (1983) J. Mol. Biol. , vol.166 , pp. 443-451
    • Henry, E.R.1    Sommer, J.H.2    Hofrichter, J.3    Eaton, W.A.4    Gellert, M.5
  • 35
    • 0026320866 scopus 로고
    • The Energy Landscapes and Motions of Proteins
    • Frauenfelder, H.; Sligar, S. G.; Wolynes, P. G. The Energy Landscapes and Motions of Proteins Science 1991, 254, 1598-1603 10.1126/science.1749933
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 37
    • 0344961407 scopus 로고    scopus 로고
    • Ligand Binding in a Docking Site of Cytochrome c Oxidase: A Time-Resolved Step-Scan Fourier Transform Infrared Study
    • Koutsoupakis, C.; Soulimane, T.; Varotsis, C. Ligand Binding in a Docking Site of Cytochrome c Oxidase: a Time-Resolved Step-Scan Fourier Transform Infrared Study J. Am. Chem. Soc. 2003, 125, 14728-14732 10.1021/ja036107e
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14728-14732
    • Koutsoupakis, C.1    Soulimane, T.2    Varotsis, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.