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J. Biol. Chem., Vol. 269, Issue 4, 2568-2573, 01, 1994
V Beckert, R Dettmer and R Bernhardt
To understand the function of the unique tyrosine in position 82 of bovine
adrenodoxin (Adx), which had been proposed to be involved in electron
transfer from NADPH-dependent adrenodoxin reductase (AdR) to cytochrome
P-450 enzymes and/or AdR binding by chemical modification studies
(Taniguchi, T., and Kimura, T. (1975) Biochemistry 14, 5573- 5578), the
residue was replaced by phenylalanine, leucine, or serine. Unchanged
absorption, CD, and electron spin resonance spectra as well as redox
potentials indicate that the environment of the [2Fe-2S] cluster was not
affected by the mutations. The Vmax values in cytochrome c reduction,
P45011A1- and P45011B1-dependent activities were also not changed when
using Y82F, Y82S, and Y82L Adx mutants as electron donor, demonstrating
that tyrosine 82 is not involved in the intra- or intermolecular electron
transfer. Replacement of tyrosine 82 did not affect AdR binding as shown by
unchanged cytochrome c activity. There are, however, changes in Km values
up to 4-fold when measuring the enzymatic activities of mutant Adx with
P45011A1 and P45011B1. These changes differ in dependence on the P-450
(P45011A1 or P45011B1) used. The results suggest that mutation of tyrosine
82 either directly or indirectly (by inducing small conformational changes
of the binding domain) affects the binding of cytochromes P-450.
Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer
Max-Delbruck-Centrum fur molekulare Medizin, Berlin-Buch, Germany.
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