Similarity of cytochrome c oxidases in different organisms

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 evolutionari...

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Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2010-09, Vol.78 (12), p.2691-2698
Main Authors: Popovic, D. M., Leontyev, I. V., Beech, D. G., Stuchebrukhov, A. A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Cattle
cytochrome c oxidase
electron transfer
Electron Transport Complex IV - chemistry
Electron Transport Complex IV - genetics
Electron Transport Complex IV - metabolism
heme-copper oxygen reductases
Models, Molecular
Molecular Sequence Data
Molecular Structure
Oxidation-Reduction
Paracoccus denitrificans - enzymology
pKa calculations
Proton Pumps - chemistry
Proton Pumps - genetics
Proton Pumps - metabolism
proton transfer
redox potentials
Rhodobacter sphaeroides - enzymology
Static Electricity
Thermodynamics
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Summary: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 (CcO) of such diverse organisms as a mammal (bovine heart mitochondrial CcO), photosynthetic bacteria (Rhodobacter sphaeroides CcO), and soil bacteria (Paracoccus denitrificans CcO) are not only structurally similar, but almost identical in microscopic electrostatics and thermodynamics properties of their key amino‐acids. By using pKa calculations of some of the key residues of the catalytic site, D‐ and K‐ proton input, and putative proton output channels of these three different enzymes, we demonstrate that the microscopic properties of key residues are almost identical, which strongly suggests the same mechanism in these species. The quantitative precision with which the microscopic physical properties of these enzymes have remained constant despite different evolutionary routes undertaken is striking. Proteins 2010. © 2010 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.22783