Ligand binding properties of bacterial oxidases in relation to cytochrome-c oxidase

1992 ◽  
Vol 20 (3) ◽  
pp. 240S-240S ◽  
Author(s):  
A. JOHN MOODY ◽  
ROBERT B. GENNIS ◽  
DAVID B. HICKS ◽  
W. JOHN INGLEDEW ◽  
TERRY ANN KRULWICH ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Binding Properties

scholarly journals ‘CO2-ligated’ cytochrome c oxidase: characterization and comparison with the Cl- -ligated enzyme

1994 ◽  
Vol 302 (3) ◽  
pp. 821-826 ◽  
Author(s):  
A J Moody ◽  
M Richardson ◽  
J P Spencer ◽  
U Brandt ◽  
P R Rich
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Absorption Spectra ◽  
Intramolecular Electron Transfer ◽  
Endogenous Ligand ◽  
Binding Properties ◽  
Visible Absorption ◽  
Bovine Heart

A form of fully oxidized bovine heart cytochrome c oxidase that is induced by CO2/HCO3- is described. The ligand-binding properties of this form are similar to those of Cl(-)-ligated oxidase [Moody, Cooper and Rich (1991) Biochim. Biophys. Acta 1059, 189-207]. Both bind cyanide at a rate (0.2 M-1.s-1 at pH 6.5) intermediate between the rate of binding to the fast and slow forms of the enzyme, and binding of formate to both is almost undetectable. They are also similar in showing poor reactivity with H2O2, or with CO in the presence of O2, which, with fast oxidase, induce the formation of the ‘ferryl’ and ‘peroxy’ states respectively. However, there is a clear difference in the near-u.v./visible absorption spectra of the two forms; that induced by CO2/HCO3- has a Soret maximum at 427 nm whereas Cl(-)-ligated oxidase has a Soret maximum similar to that of fast oxidase at about 424 nm. It appears that both CO2/HCO3- and Cl- are members of a class of ligands that lowers the reactivity of the binuclear centre but does not impede intramolecular electron transfer from haem a to the binuclear centre, unlike the putative endogenous ligand responsible for slow oxidase.

scholarly journals Time-resolved infrared studies of the dynamics of ligand binding to cytochrome c oxidase

1991 ◽  
Author(s):  
R. B. Dyer ◽  
Kristen A. Peterson ◽  
Page O. Stoutland ◽  
Oloef Einarsdottir ◽  
William H. Woodruff
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Time Resolved ◽  
Infrared Studies

An Intermediate Conformational State during Ligand Binding to Cytochrome c Oxidase Detected by Time-resolved Resonance Raman Analyses of Heme Peripheral Groups

2012 ◽  
Vol 41 (2) ◽  
pp. 178-180 ◽  
Author(s):  
Izumi Ishigami ◽  
Takeshi Nishigaki ◽  
Kyoko Shinzawa-Itoh ◽  
Shinya Yoshikawa ◽  
Satoru Nakashima ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Resonance Raman ◽  
Conformational State ◽  
Time Resolved

scholarly journals Change in structure and ligand binding properties of hyperstable cytochrome c 555 from A quifex aeolicus by domain swapping

2015 ◽  
Vol 24 (3) ◽  
pp. 366-375 ◽  
Author(s):  
Masaru Yamanaka ◽  
Satoshi Nagao ◽  
Hirofumi Komori ◽  
Yoshiki Higuchi ◽  
Shun Hirota
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Domain Swapping ◽  
Binding Properties

scholarly journals The Ligand Binding Battle at Cytochrome c Oxidase

2009 ◽  
Vol 104 (10) ◽  
pp. 1136-1138 ◽  
Author(s):  
Mark T. Gladwin ◽  
Sruti Shiva
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase
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