Abstract：
:Phenylalanine 87 of Bacillus megaterium cytochrome P450 BM3, a residue close to the heme in the substrate binding pocket, has been replaced by alanine by site-directed mutagenesis. The substitution had no effect on the rate of hydroxylation of laurate and increased the affinity for laurate of both the intact enzyme and its heme domain by 2.6-6-fold in the ferric state. NMR paramagnetic relaxation measurements showed that in the initial ferric enzyme-substrate complex, where the substrate binds relatively far from the heme, the substitution had no effect on the position or orientation of the bound substrate. However, in the next intermediate in the catalytic cycle, the reduced enzyme, the position of the bound substrate was altered so that the terminal methyl group was 3.1 A from the iron in the mutant, compared to 5.1 A in the wild-type enzyme. Analysis of the products of the action of the enzyme on laurate and myristate showed that the mutant catalyzed hydroxylation almost exclusively at the omega position, in marked contrast to the wild-type enzyme, with which no hydroxylation at this position was observed.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Oliver CF,Modi S,Sutcliffe MJ,Primrose WU,Lian LY,Roberts GCdoi
10.1021/bi962826csubject
Has Abstractpub_date
1997-02-18 00:00:00pages
1567-72issue
7eissn
0006-2960issn
1520-4995pii
bi962826cjournal_volume
36pub_type
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