Abstract:
:The Escherichia coli cytochrome bo is a heme-copper terminal ubiquinol oxidase, and functions as a redox-driven proton pump. We applied pulse radiolysis technique for studying the one-electron reduction processes in the Cu(B)-deficient mutant, His333Ala. We found that the Cu(B) deficiency suppressed the heme b-to-heme o electron transfer two order of the magnitude (4.0 x 10(2) s(-1)), as found for the wild-type enzyme in the presence of 1 mM KCN (3.0 x 10(2) s(-1)). Potentiometric analysis of the His333Ala mutant revealed the 40 mV decrease in the E(m) value for low-spin heme b and the 160 mV increase in the E(m) value of high-spin heme o. Our results indicate that Cu(B) not only serves as one-electron donor to the bound dioxygen upon the O-O bond cleavage, but also facilitates dioxygen reduction at the heme-copper binuclear centre by modulating the E(m) value of heme o through magnetic interactions. And the absence of a putative OH(-) bound to Cu(B) seems not to affect the uptake of the first chemical proton via K-channel in the His333Ala mutant.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Kobayashi K,Tagawa S,Mogi Tdoi
10.1093/jb/mvp026subject
Has Abstractpub_date
2009-05-01 00:00:00pages
685-91issue
5eissn
0021-924Xissn
1756-2651pii
mvp026journal_volume
145pub_type
杂志文章abstract::We identified a protein with a molecular weight of about 44 kDa in an extract of rat regenerating liver. This protein was undetectable in normal, sham-operated, and completely regenerated liver. We also purified this 44-kDa protein from an extract of rat liver remnant after partial hepatectomy. The partial amino acid ...
journal_title:Journal of biochemistry
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更新日期:1997-03-01 00:00:00
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a021439
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journal_title:Journal of biochemistry
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更新日期:1994-10-01 00:00:00