Binuclear centre structure of terminal protonmotive oxidases

The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS Letters 1993-02, Vol.316 (3), p.216-223
Hauptverfasser:	Brown, Simon, Moody, A.John, Mitchell, Roy, Rich, Peter R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Bacterial Proteins - chemistry Biological and medical sciences Biophysical Phenomena Biophysics Catalysis Cattle Cytochrome b Group - chemistry Cytochrome bo Cytochrome c oxidase Electron Transport Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Heme - chemistry Ion Channels Molecular Sequence Data Oxidation-Reduction Oxidoreductases Protein Conformation Protein Structure, Tertiary Protons Sequence Alignment Sequence conservation structure
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319, T326) into the vicinity of the binuclear centre, suggestive of a proton-transferring function. In addition, we also consider those residues which may participate in electron transport between Cu A and haem a. We suggest several potential lines of investigation.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(93)81296-C