Mutagenesis, site-directed flavocytochrome

Tyr 143, 36 293 Tyr 254, 36 291-293 NMR spectroscopy, 36 271-272 pH dependence, 36 274-275 primary stmcture, 36 261-263 prosthetic groups structure, 36 258 quaternary structure, 36 261-262 reduction potentials, 36 268-269 short electron transport chain, 36 258-259 site-directed mutagenesis, 36 289-290 substrate specificity, 36 272-274 Flavocytochrome C552 electrochemistry, 36 365-367, 369... 

The high-level expression of recombinant flavocytochrome 7>2 in E. call (Black et al., 1989) has allowed the active site of the enzyme to be probed using site-directed mutagenesis. Two particular residues, His373 and Tyr254, have been examined in detail, since they have important roles in catalysis. The substitution of His373 by glutamine resulted in an enzyme with some... 

The model proposed by Short et al. (1998) has been rigorously tested by site-directed mutagenesis and kinetic analysis of the mutant enzymes. It has been shown to be consistent with all of the results from these studies and therefore it may indeed represent the physiological complex formed between flavocytochrome 4 2 cytochrome c. 

Muonium chemistry gaseous phase, 28 119-120 liquid mixtures, 28 120-122 radical formation and reactions, 28 122-130 Mushrooms, vanadium in, 35 96-97 Mutagenesis, site-directed, flavocytochrome bj, 36 289-290 MXj-... 

Several point mutations in the S. cerevisiae flavocytochrome coding sequence have been constructed by oligonucleotide-directed site-specific mutagenesis of the cloned gene (143). The enzyme-coding region was transferred to a plasmid designed both for expression of... 

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