Abstract:
:Cytochrome ba3 from Thermus thermophilus reacts slowly with excess HCN at pH 7.4 to create a form of the enzyme in which CuA, cytochrome b, and CuB remain oxidized, while cytochrome a3 is reduced by one electron, presumably with the formation of cyanogen. We have examined this form of the enzyme by UV-visible, resonance Raman, EPR, and electron nuclear double resonance spectroscopies in conjunction with permutations of 13C- and 15N-labeled cyanide. The results support a model in which one CN- binds through the carbon atom to ferrous a3, supporting a low-spin (S = 0) configuration on the Fe; bridging by this cyanide to the CuB is weak or absent. Four 14N atoms, presumably donated by histidine residues of the protein, provide a strong equatorial ligand field about CuB; a second CN- is coordinated through the carbon atom to CuB in an axial position.
journal_name
Proc Natl Acad Sci U S Aauthors
Surerus KK,Oertling WA,Fan C,Gurbiel RJ,Einarsdóttir O,Antholine WE,Dyer RB,Hoffman BM,Woodruff WH,Fee JAdoi
10.1073/pnas.89.8.3195keywords:
subject
Has Abstractpub_date
1992-04-15 00:00:00pages
3195-9issue
8eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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