Abstract:
:Cytochrome bd is a bacterial respiratory oxidase carrying three hemes but no copper. We show that nitric oxide (NO) reacts with the intermediate F of cytochrome bd from Azotobacter vinelandii: (i) with a 1:1 stoichiometry, (ii) rapidly (k=1.2 +/- 0.1 x 10(5)M(-1)s(-1) at 20 degrees C), and (iii) yielding the oxidized enzyme with nitrite bound to heme d at the active site. Unexpectedly, the NO reaction mechanism of this catalytic intermediate in the Cu(B)-lacking cytochrome bd appears similar to that of beef heart cytochrome c oxidase, where Cu(B) was proposed to play a key role.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Borisov VB,Forte E,Sarti P,Brunori M,Konstantinov AA,Giuffrè Adoi
10.1016/j.febslet.2006.07.072subject
Has Abstractpub_date
2006-09-04 00:00:00pages
4823-6issue
20eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00928-8journal_volume
580pub_type
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