Electron Carriers of Cytochrome Oxidase Detectable by Electron Paramagnetic Resonance and their Relationship to those Traditionally Recognized in this Enzyme

On the basis of oxidoreductive rapid kinetic and titration experiments with purified cytochrome c oxidase (EC 1.9.3.1), monitored by electron paramagnetic resonance (EPR) at 13 degrees K and by spectrophotometry at 100 degrees K, a new assignment of EPR signals is proposed. The bulk of both the low-...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1973-09, Vol.70 (9), p.2477-2481
Main Authors: Hartzell, Charles R., Hansen, Raymond E., Beinert, Helmut
Format: Article
Language:English
Subjects:
Absorption spectra
Biological Sciences: Biochemistry
Copper
Cytochromes
Electron Transport Complex IV
Electrons
Enzymes
Heme
Kinetics
Ligands
Magnetic Resonance Spectroscopy
Oxidases
Oxidation-Reduction
Signal detection
Signal reflection
Spectral reflectance
Spectrophotometry
Titration
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:On the basis of oxidoreductive rapid kinetic and titration experiments with purified cytochrome c oxidase (EC 1.9.3.1), monitored by electron paramagnetic resonance (EPR) at 13 degrees K and by spectrophotometry at 100 degrees K, a new assignment of EPR signals is proposed. The bulk of both the low-spin (g = 3.0; 2.2; 1.5) and high-spin (g = 6; 2) signals is attributed to the component with the properties of traditional cytochrome a. It is further proposed that the absorption band at 655 nm represents the most unambiguous manifestation of the a3component.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.70.9.2477