Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference47 articles.
1. Structural features of cytochrome oxidase
2. Structure of the heme o prosthetic group from the terminal quinol oxidase of Escherichia coli
3. Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity
4. The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type
5. Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the Escherichia coli cytochrome o complex is in subunit I.
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