Structure and Electrochemical Studies of [(trispicMeen)ClFeIIIOFeIIICl(trispicMeen)]2+. Spectroscopic Characterization of the Mixed-Valence FeIIIOFeIIForm. Relevance to the Active Site of Dinuclear Iron−Oxo Proteins

1997 ◽  
Vol 36 (5) ◽  
pp. 846-853 ◽  
Author(s):  
Alexander L. Nivorozhkin ◽  
Elodie Anxolabéhère-Mallart ◽  
Pierre Mialane ◽  
Roman Davydov ◽  
Jean Guilhem ◽  
...  
2007 ◽  
Vol 101 (7) ◽  
pp. 1043-1048 ◽  
Author(s):  
Boris Bleijlevens ◽  
Tara Shivarattan ◽  
Barbara Sedgwick ◽  
Stephen E.J. Rigby ◽  
Steve J. Matthews

2002 ◽  
Vol 30 (4) ◽  
pp. 653-658 ◽  
Author(s):  
R. S. Pitcher ◽  
T. Brittain ◽  
N. J. Watmugh

Cytochrome cbb3 oxidase is a member of the haem-copper oxidase superfamily. It is characterized by its high oxygen affinity, while retaining the ability to pump protons. These attributes are central to its proposed role in bacterial microaerobic metabolism. Recent spectroscopic characterization of both the cytochrome cbb3 oxidase complex from Pseudomonas stutzeri and the dihaem ccoP subunit expressed separately in Escherichia coli has revealed the presence of a low-spin His/His co-ordinated c-type cytochrome. The low midpoint reduction potential of this haem (Em < + 100 mV), together with its unexpected ability to bind CO in the reduced state at the expense of the distal histidine ligand, raises questions about the role of the ccoP subunit in the delivery of electrons to the active site.


1989 ◽  
Vol 36 (3-4) ◽  
pp. 245
Author(s):  
J.L. Cole ◽  
E.K. Yang ◽  
P.O. Sandusky ◽  
E.I. Solomon

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