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Similarity of Cytochrome C Oxidases in Different Organisms by D. M. Popovic; I. V. Leontyev; D. G. Beech; A. A. Stuchebrukhov is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Similarity of Cytochrome C Oxidases in Different Organisms about?

## Abstract Most of biological oxygen reduction is catalyzed by the heme‐copper oxygen reductases. These enzymes are redox‐driven proton pumps that take part in generating the proton gradient in both prokaryotes and mitochondria that drives synthesis of ATP. The enzymes have been divided into three evolutionarily‐related groups: the A‐, B‐, and C‐families. Recent comparative studies suggest that all oxygen reductases perform the same chemistry for oxygen reduction and comprise the same essential elements of the proton pumping mechanism, such as the proton loading and kinetic gating sites, which, however, appear to be different in different families. All species of the A‐family, however, demonstrate remarkable similarity of the central processing unit of the enzyme, as revealed by their recent crystal structures. Here we demonstrate that cytochrome __c__ oxidases (C__c__O) of such diverse organisms as a mammal (bovine heart mitochondrial C__c__O), photosynthetic bacteria (__Rhodobacter sphaeroides__ C__c__O), and soil bacteria (__Paracoccus denitrificans__ C__c__O) are not only structurally similar, but almost identical in microscopic electrostatics and thermodynamics properties of

Who reads Similarity of Cytochrome C Oxidases in Different Organisms?

Author

D. M. Popovic; I. V. Leontyev; D. G. Beech; A. A. Stuchebrukhov

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)