ISSN:
1573-6881
Keywords:
Heme ligands
;
Cu ligands
;
proton pumping
;
mitochondrial cytochromec oxidase
;
COFTIR
;
oxidase superfamily
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract Cytochromeaa 3 ofRhodobacter sphaeroides and cytochromebo ofE. coli are useful models of the more complex cytochromec oxidase of eukaryotes, as demonstrated by the genetic, spectroscopic, and functional studies reviewed here. A summary of site-directed mutants of conserved residues in these two enzymes is presented and discussed in terms of a current model of the structure of the metal centers and evidence for regions of the protein likely to be involved in proton transfer. The model of ligation of the hemea 3 (oro)-CuB center, in which both hemes are bound to helix X of subunit I, has important implications for the pathways and control of electron transfer.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00762854
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