A structural and functional perspective on the evolution of the heme-copper oxidases

Vivek Sharma; Mårten Wikström

doi:10.1016/j.febslet.2014.09.020

A structural and functional perspective on the evolution of the heme-copper oxidases

FEBS Lett. 2014 Nov 3;588(21):3787-92. doi: 10.1016/j.febslet.2014.09.020. Epub 2014 Sep 26.

Authors

Vivek Sharma¹, Mårten Wikström²

Affiliations

¹ Department of Physics, Tampere University of Technology, PO Box 692, FI-33101 Tampere, Finland. Electronic address: vivek.sharma@tut.fi.
² Helsinki Bioenergetics Group, Institute of Biotechnology, University of Helsinki, FI-00014 Helsinki, Finland.

PMID: 25261254
DOI: 10.1016/j.febslet.2014.09.020

Abstract

The heme-copper oxidases (HCOs) catalyze the reduction of O2 to water, and couple the free energy to proton pumping across the membrane. HCOs are divided into three sub-classes, A, B and C, whose order of emergence in evolution has been controversial. Here we have analyzed recent structural and functional data on HCOs and their homologues, the nitric oxide reductases (NORs). We suggest that the C-type oxidases are ancient enzymes that emerged from the NORs. In contrast, the A-type oxidases are the most advanced from both structural and functional viewpoints, which we interpret as evidence for having evolved later.

Keywords: Cytochrome c oxidase; Electron transfer; Nitric oxide reductase; Proton pumping.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Evolution, Molecular*
Heme / metabolism*
Models, Molecular
Oxidoreductases / chemistry*
Oxidoreductases / metabolism*
Protein Conformation
Tyrosine

Substances

Tyrosine
Heme
Oxidoreductases
copper oxidase
nitric-oxide reductase