Heme/copper terminal oxidases
Article Abstract:
The heme/copper containing oxidases catalyze the reduction of dioxygen to water, and the coupling of the free energy released for proton translocations. The reduction of dioxygen to water removes low-energy electrons from the respiratory system. This allows electron transfer and free-energy transduction. The terminal heme/copper oxidases function according to thermodynamic and structural principles in respiratory electron-transfer chains. The reaction follows a concerted mechanism, which allows the terminal oxidases to operate as redox-linked proton pumps.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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Iron-sulfur proteins with nonredox functions
Article Abstract:
Proteins bound to the iron-sulfur (Fe-S) cluster prosthetic groups in cytosolic aconitase/iron-responsive element binding protein exhibit nonredox functions. The Fe-S clusters participate in electron transport reactions, catalysis, and control of the proteins' structure and their regulation. Escherichia coli has three fumarase genes, FumA, FumB and FumC that use Fe-S clusters to play multiple roles. FumA and FumB are sensitive to O2-, which make Fe-S clusters in these genes favourable for additional functions besides catalysis.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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Protein structure and the energetics of protein stability
Article Abstract:
The relationship of protein stability and protein structure established by thermodynamic parameters were analyzed. Calorimetric and spectroscopic studies and structural models from X-ray crystallography and nuclear magnetic resonance spectroscopy were used to derive the parameters. Regular features of the structure such as, solvent-exposed surface areas, secondary structure content, and numbers of disulfide bonds were considered.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1997
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