Spectroscopic and Kinetic Studies ofArabidopsisthalianaSulfite Oxidase: Nature of the Redox-Active Orbital and Electronic Structure Contributions to Catalysis

2005 ◽  
Vol 127 (47) ◽  
pp. 16567-16577 ◽  
Author(s):  
Craig Hemann ◽  
Brian L. Hood ◽  
Meita Fulton ◽  
Robert Hänsch ◽  
Günter Schwarz ◽  
...  
2016 ◽  
Vol 45 (40) ◽  
pp. 15828-15839 ◽  
Author(s):  
Sven Wiesner ◽  
Arne Wagner ◽  
Elisabeth Kaifer ◽  
Hans-Jörg Himmel

The electronic structures of dinuclear copper complexes of the general formula [GFA(CuX2)2], where X = Br or Cl and GFA denotes a redox-active bridging Guanidino-Functionalized Aromatic ligand, were analysed and compared.


2010 ◽  
Vol 49 (12) ◽  
pp. 5686-5700 ◽  
Author(s):  
Corinna R. Hess ◽  
Thomas Weyhermüller ◽  
Eckhard Bill ◽  
Karl Wieghardt

1987 ◽  
Vol 246 (2) ◽  
pp. 455-465 ◽  
Author(s):  
G A Ashby ◽  
R N F Thorneley

The kinetics of reduction of indigocarmine-dye-oxidized Fe protein of nitrogenase from Klebsiella pneumoniae (Kp2ox) by sodium dithionite in the presence and absence of MgADP were studied by stopped-flow spectrophotometry at 23 degrees C and at pH 7.4. Highly co-operative binding of 2MgADP (composite K greater than 4 × 10(10) M-2) to Kp2ox induced a rapid conformation change which caused the redox-active 4Fe-4S centre to be reduced by SO2-.(formed by the predissociation of dithionite ion) with k = 3 × 10(6) M-1.s-1. This rate constant is at least 30 times lower than that for the reduction of free Kp2ox (k greater than 10(8) M-1.s-1). Two mechanisms have been considered and limits obtained for the rate constants for MgADP binding/dissociation and a protein conformation change. Both mechanisms give rate constants (e.g. MgADP binding 3 × 10(5) less than k less than 3 × 10(6) M-1.s-1 and protein conformation change 6 × 10(2) less than k less than 6 × 10(3) s-1) that are similar to those reported for creatine kinase (EC 2.7.3.2). The kinetics also show that in the catalytic cycle of nitrogenase with sodium dithionite as reductant replacement of 2MgADP by 2MgATP occurs on reduced and not oxidized Kp2. Although the Kp2ox was reduced stoichiometrically by SO2-. and bound two equivalents of MgADP with complete conversion into the less-reactive conformation, it was only 45% active with respect to its ability to effect MgATP-dependent electron transfer to the MoFe protein.


2012 ◽  
Vol 52 (2) ◽  
pp. 898-909 ◽  
Author(s):  
Stacey Lindsay ◽  
Siu K. Lo ◽  
Oliver R. Maguire ◽  
Eckhard Bill ◽  
Michael R. Probert ◽  
...  

2015 ◽  
Vol 44 (44) ◽  
pp. 19111-19125 ◽  
Author(s):  
Alexandra Ziesak ◽  
Tobias Wesp ◽  
Olaf Hübner ◽  
Elisabeth Kaifer ◽  
Hubert Wadepohl ◽  
...  

Decision-making counter-ligands: a bridging redox-active ligand in a dinuclear copper complex could be either neutral (complex type [CuII-GFA-CuII]) or dicationic (complex type [CuI-GFA-CuI]), depending on the nature of the counter-ligands X.


2010 ◽  
Vol 49 (4) ◽  
pp. 1995-2007 ◽  
Author(s):  
Eric J. Schelter ◽  
Ruilian Wu ◽  
Jacqueline M. Veauthier ◽  
Eric D. Bauer ◽  
Corwin H. Booth ◽  
...  

Polyhedron ◽  
2016 ◽  
Vol 108 ◽  
pp. 2-7 ◽  
Author(s):  
Molina A.L. Sheepwash ◽  
Alan J. Lough ◽  
Lorenzo Poggini ◽  
Giordano Poneti ◽  
Martin T. Lemaire

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