Dioxygen Activation at Non-Heme Iron: Insights from Rapid Kinetic Studies

ChemInform ◽  
2007 ◽  
Vol 38 (40) ◽  
Author(s):  
Ivan V. Korendovych ◽  
Sergey V. Kryatov ◽  
Elena V. Rybak-Akimova
Keyword(s):  
Kinetic Studies ◽  
Heme Iron ◽  
Dioxygen Activation ◽  
Non Heme Iron

Dioxygen Activation at Non-Heme Iron: Insights from Rapid Kinetic Studies

2007 ◽  
Vol 40 (7) ◽  
pp. 510-521 ◽  
Author(s):  
Ivan V. Korendovych ◽  
Sergey V. Kryatov ◽  
Elena V. Rybak-Akimova
Keyword(s):  
Kinetic Studies ◽  
Heme Iron ◽  
Dioxygen Activation ◽  
Non Heme Iron

Dioxygen Activation by a Non-Heme Iron(II) Complex: Theoretical Study toward Understanding Ferric–Superoxo Complexes

2012 ◽  
Vol 8 (3) ◽  
pp. 915-926 ◽  
Author(s):  
Hui Chen ◽  
Kyung-Bin Cho ◽  
Wenzhen Lai ◽  
Wonwoo Nam ◽  
Sason Shaik
Keyword(s):  
Theoretical Study ◽  
Heme Iron ◽  
Dioxygen Activation ◽  
Non Heme Iron

Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters

1996 ◽  
Vol 96 (7) ◽  
pp. 2625-2658 ◽  
Author(s):  
Bradley J. Wallar ◽  
John D. Lipscomb
Keyword(s):  
Heme Iron ◽  
Dioxygen Activation ◽  
Iron Clusters ◽  
Non Heme Iron

Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites

1996 ◽  
Vol 96 (7) ◽  
pp. 2607-2624 ◽  
Author(s):  
Lawrence Que ◽  
Raymond Y. N. Ho
Keyword(s):  
Active Sites ◽  
Heme Iron ◽  
Dioxygen Activation ◽  
Non Heme Iron ◽  
Iron Active Sites

MECHANISM OF Fe++-CYTOCROME c REDUCTASE OF FERROBACILLUS FERROOXIDANS

1967 ◽  
Vol 45 (10) ◽  
pp. 1547-1556 ◽  
Author(s):  
George A. Din ◽  
Isamu Suzuki
Keyword(s):  
Cytochrome C ◽  
Kinetic Studies ◽  
Product Inhibition ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Oxidation Reduction ◽  
Dead End ◽  
Ping Pong ◽  
Stable Forms ◽  
Variable Substrate

The mechanism of Fe++-cytochrome c reductase was investigated. Kinetic studies on initial velocity and product inhibition, as well as spectrofluorometric studies, were consistent with a Ping Pong Bi Bi mechanism with two stable forms of enzyme. The Km values for the substrates were found to be 0.59 mM for Fe++ and 0.085 mM for cytochrome c. The inhibition constants for Fe+++ and reduced cytochrome c were 0.137 mM and 0.0135 mM, respectively. The oxidation–reduction of non-heme iron bound to the enzyme protein was implicated as the responsible factor for the oscillation of the enzyme between its two forms. NaCl was a dead-end inhibitor binding the ferrous form of the enzyme, showing an uncompetitive inhibition with Fe++ as a variable substrate.

Sign in / Sign up

Export Citation Format

Share Document