Affiliation:
1. Max-Planck-Institut für Biophysik, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany.
Abstract
C-Family Oxidase Structure
The heme-copper oxidases (HCOs) play a key role in aerobic respiration by coupling oxygen reduction to transmembrane proton pumping to generate electrochemical ion gradients across biological membranes that provide energy for many cellular processes. Based on subunit composition, electron donor, and heme type, the HCOs are divided into three families, of which families A and B have been structurally characterized.
Buschmann
et al.
(p.
327
, published online 24 June) now report the crystal structure of the C-family
cbb3
oxidase from
Pseudomonas stutzeri
. The structure suggests a different redox-driven pumping mechanism from A and B HCOs, and gives insight into why C HCOs are catalytically active at low oxygen concentrations.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
226 articles.
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